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Penicillin
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For the Japanese band, see Penicillin (band).
Penicillin
Penicillin core structure, where "R" is the variable group
Clinical data
AHFS/Drugs.com
Micromedex Detailed Consumer Information
Pregnancy
category
US: B (No risk in non-human studies) [1]
Routes of
administration
Intravenous, intramuscular, by mouth
Legal status
Legal status
In general: ℞ (Prescription only)
Pharmacokinetic data
Metabolism
liver
Biological half-life
between 0.5 and 56 hours
Excretion
Kidneys
Identifiers
ChemSpider
none
Chemical and physical data
Formula
C9H11N2O4S
Molar mass
243.26 g·mol−1
Penicillin (PCN or pen) is a group of antibiotics which include penicillin G (intravenous use), penicillin V (use by mouth), procaine penicillin, and benzathine penicillin (intramuscular use). Penicillin antibiotics were among the first medications to be effective against many bacterial infections caused by staphylococci and streptococci. They are still widely used today, though many types of bacteria have developed resistance following extensive use.
About 10% of people report that they are allergic to penicillin; however, up to 90% of this group may not actually be allergic.[2] Serious allergies only occur in about 0.03%.[2] All penicillins are β-lactam antibiotics.
Penicillin was discovered in 1928 by Scottish scientist Alexander Fleming.[3] People began using it to treat infections in 1942.[4] There are several enhanced penicillin families which are effective against additional bacteria; these include the antistaphylococcal penicillins, aminopenicillins and the antipseudomonal penicillins. They are derived from Penicillium fungi.[5]
Contents
[hide]
1 Medical uses
1.1 Susceptibility
2 Side effects
3 Mechanism of action
4 Structure
5 History
5.1 Discovery
5.2 Medical application
5.3 Mass production
5.4 Structure determination and total synthesis
5.5 Developments from penicillin
6 Production
6.1 Biosynthesis
7 Members
7.1 Natural penicillins
7.2 β-lactamase-resistant
7.3 Aminopenicillins
7.4 Carboxypenicillins
7.5 Ureidopenicillins
7.6 β-lactamase inhibitors
8 See also
9 Notes
10 References
11 External links
Medical uses[edit]
The term "penicillin" is often used generically to refer to benzylpenicillin (penicillin G, the original penicillin found in 1928), procaine benzylpenicillin (procaine penicillin), benzathine benzylpenicillin (benzathine penicillin), and phenoxymethylpenicillin (penicillin V). Procaine penicillin and benzathine penicillin have the same antibacterial activity as benzylpenicillin but act for a longer period of time. Phenoxymethylpenicillin is less active against gram-negative bacteria than benzylpenicillin.[6][7] Benzylpenicillin, procaine penicillin and benzathine penicillin can be given by intravenous or intramuscular injections, but phenoxymethylpenicillin can be given by mouth because of its acidic stability.[8]
Susceptibility[edit]
While the number of penicillin-resistant bacteria is increasing, penicillin can still be used to treat a wide range of infections caused by certain susceptible bacteria, including Streptococci, Staphylococci, Clostridium, and Listeria genera. The following list illustrates minimum inhibitory concentration susceptibility data for a few medically significant bacteria:[9][10]
Listeria monocytogenes: from less than or equal to 0.06 μg/ml to 0.25 μg/ml
Neisseria meningitidis: from less than or equal to 0.03 μg/ml to 0.5 μg/ml
Staphylococcus aureus: from less than or equal to 0.015 μg/ml to more than 32 μg/ml
Side effects[edit]
Main article: Side effects of penicillin
Common (≥ 1% of people) adverse drug reactions associated with use of the penicillins include diarrhoea, hypersensitivity, nausea, rash, neurotoxicity, urticaria, and superinfection (including candidiasis). Infrequent adverse effects (0.1–1% of people) include fever, vomiting, erythema, dermatitis, angioedema, seizures (especially in people with epilepsy), and pseudomembranous colitis.[11] Penicillin can also induce serum sickness or a serum sickness-like reaction in some individuals. Serum sickness is a type III hypersensitivity reaction that occurs one to three weeks after exposure to drugs including penicillin. It is not a true drug allergy, because allergies are type I hypersensitivity reactions, but repeated exposure to the offending agent can result in an anaphylactic reaction.[medical citation needed] Anaphylaxis will occur in approximately 0.01% of patients.[11]
Pain and inflammation at the injection site is also common for parenterally administered benzathine benzylpenicillin, benzylpenicillin, and, to a lesser extent, procaine benzylpenicillin.[medical citation needed]
Mechanism of action[edit]
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Main article: Beta-lactam antibiotic
Bacteria that attempt to grow and divide in the presence of penicillin fail to do so, and instead end up shedding their cell walls.
Penicillin and other β-lactam antibiotics act by inhibiting penicillin-binding proteins, which normally catalyze cross-linking of bacterial cell walls.
Bacteria constantly remodel their peptidoglycan cell walls, simultaneously building and breaking down portions of the cell wall as they grow and divide. β-Lactam antibiotics inhibit the formation of peptidoglycan cross-links in the bacterial cell wall; this is achieved through binding of the four-membered β-lactam ring of penicillin to the enzyme DD-transpeptidase. As a consequence, DD-transpeptidase cannot catalyze formation of these cross-links, and an imbalance between cell wall production and degradation develops, causing the cell to rapidly die.
The enzymes that hydrolyze the peptidoglycan cross-links continue to function, even while those that form such cross-links do not. This weakens the cell wall of the bacterium, and osmotic pressure becomes increasingly uncompensated—eventually causing cell death (cytolysis). In addition, the build-up of peptidoglycan precursors triggers the activation of bacterial cell wall hydrolases and autolysins, which further digest the cell wall's peptidoglycans. The small size of the penicillins increases their potency, by allowing them to penetrate the entire depth of the cell wall. This is in contrast to the glycopeptide antibiotics vancomycin and teicoplanin, which are both much larger than the penicillins.[12]
Gram-positive bacteria are called protoplasts when they lose their cell walls. Gram-negative bacteria do not lose their cell walls completely and are called spheroplasts after treatment with penicillin.
Penicillin shows a synergistic effect with aminoglycosides, since the inhibition of peptidoglycan synthesis allows aminoglycosides to penetrate the bacterial cell wall more easily, allowing their disruption of bacterial protein synthesis within the cell. This results in a lowered MBC for susceptible organisms.[13]
Penicillins, like other β-lactam antibiotics, block not only the division of bacteria, including cyanobacteria, but also the division of cyanelles, the photosynthetic organelles of the glaucophytes, and the division of chloroplasts of bryophytes. In contrast, they have no effect on the plastids of the highly developed vascular plants. This supports the endosymbiotic theory of the evolution of plastid division in land plants.[14]
The chemical structure of penicillin is triggered with a very precise, pH-dependent directed mechanism, effected by a unique spatial assembly of molecular components, which can activate by protonation. It can travel through bodily fluids, targeting and inactivating enzymes responsible for cell-wall synthesis in gram-positive bacteria, meanwhile avoiding the surrounding non-targets. Penicillin can protect itself from spontaneous hydrolysis in the body in its anionic form, while storing its potential as a strong acylating agent, activated only upon approach to the target transpeptidase enzyme and protonated in the active centre. This targeted protonation neutralizes the carboxylic acid moiety, which is weakening of the β-lactam ring N–C(=O) bond, resulting in a self-activation. Specific structural requirements are equated to constructing the perfect mouse trap for catching targeted prey.[15]
Structure[edit]
Chemical structure of Penicillin G. The sulfur and nitrogen of the five-membered thiazolidine ring are shown in yellow and blue respectively. The image shows that the thiazolidine ring and fused four-membered β-lactam are not in the same plane.
The term "penam" is used to describe the common core skeleton of a member of the penicillins. This core has the molecular formula R-C9H11N2O4S, where R is the variable side chain that differentiates the penicillins from one another. The penam core has a molar mass of 243 g/mol, with larger penicillins having molar mass near 450—for example, cloxacillin has a molar mass of 436 g/mol. The key structural feature of the penicillins is the four-membered β-lactam ring; this structural moiety is essential for penicillin's antibacterial activity. The β-lactam ring is itself fused to a five-membered thiazolidine ring. The fusion of these two rings causes the β-lactam ring to be more reactive than monocyclic β-lactams because the two fused rings distort the β-lactam amide bond and therefore remove the resonance stabilisation normally found in these chemical bonds.[16]
History[edit]
Discovery[edit]
Main article: History of penicillin
Alexander Fleming, who is credited with discovering penicillin in 1928.
Sample of penicillium mould presented by Alexander Fleming to Douglas Macleod, 1935
Starting in the late 19th century there had been many accounts by scientists and physicians on the antibacterial properties of the different types of moulds including the mould penicillium but they were unable to discern what process was causing the effect.[17] The effects of penicillium mould would finally be isolated in 1928 by Scottish scientist Alexander Fleming, in work that seems to have been independent of those earlier observations.[18] Fleming recounted that the date of his discovery of penicillin was on the morning of Friday 28 September 1928.[19] The traditional version of this story describes the discovery as a serendipitous accident: in his laboratory in the basement of St Mary's Hospital in London (now part of Imperial College), Fleming noticed a Petri dish containing Staphylococcus that had been mistakenly left open was contaminated by blue-green mould from an open window, which formed a visible growth.[20] There was a halo of inhibited bacterial growth around the mould. Fleming concluded that the mould released a substance that repressed the growth and caused lysing of the bacteria.[21]
Once Fleming made his discovery he grew a pure culture and discovered it was a Penicillium mould, now known as Penicillium chrysogenum. Fleming coined the term "penicillin" to describe the filtrate of a broth culture of the Penicillium mould. Fleming asked C. J. La Touche to help identify the mould, which he incorrectly identified as Penicillium rubrum (later corrected by Charles Thom). He expressed initial optimism that penicillin would be a useful disinfectant, because of its high potency and minimal toxicity in comparison to antiseptics of the day, and noted its laboratory value in the isolation of Bacillus influenzae (now called Haemophilus influenzae).[20][22]
Fleming was a famously poor communicator and orator, which meant his findings were not initially given much attention.[20] He was unable to convince a chemist to help him extract and stabilize the antibacterial compound found in the broth filtrate. Despite this, he remained interested in the potential use of penicillin and presented a paper entitled "A Medium for the Isolation of Pfeiffer's Bacillus" to the Medical Research Club of London, which was met with little interest and even less enthusiasm by his peers. Had Fleming been more successful at making other scientists interested in his work, penicillin for medicinal use would possibly have been developed years earlier.[20]
Despite the lack of interest of his fellow scientists, he did conduct several experiments on the antibiotic substance he discovered. The most important result proved it was nontoxic in humans by first performing toxicity tests in animals and then on humans. His following experiments on penicillin's response to heat and pH allowed Fleming to increase the stability of the compound.[22] The one test that modern scientists would find missing from his work was the test of penicillin on an infected animal, the results of which would likely have sparked great interest in penicillin and sped its development by almost a decade.[20]
Medical application[edit]
Florey (pictured), Fleming and Chain shared a Nobel Prize in 1945 for their work on penicillin.
In 1930, Cecil George Paine, a pathologist at the Royal Infirmary in Sheffield, attempted to use penicillin to treat sycosis barbae, eruptions in beard follicles, but was unsuccessful. Moving on to ophthalmia neonatorum, a gonococcal infection in infants, he achieved the first recorded cure with penicillin, on November 25, 1930. He then cured four additional patients (one adult and three infants) of eye infections, and failed to cure a fifth.[23][24][25]
In 1939, Australian scientist Howard Florey (later Baron Florey) and a team of researchers (Ernst Boris Chain, Edward Abraham, Arthur Duncan Gardner, Norman Heatley, M. Jennings, J. Orr-Ewing and G. Sanders) at the Sir William Dunn School of Pathology, University of Oxford made progress in showing the in vivo bactericidal action of penicillin.[26][27] In 1940, they showed that penicillin effectively cured bacterial infection in mice.[28][29] In 1941, they treated a policeman, Albert Alexander, with a severe face infection; his condition improved, but then supplies of penicillin ran out and he died. Subsequently, several other patients were treated successfully.[30] In December 1942, survivors of the Cocoanut Grove fire in Boston were the first burn patients to be successfully treated with penicillin.[31]
Mass production[edit]
A technician preparing penicillin in 1943
By late 1940, the Oxford team under Howard Florey had devised a method of mass-producing the drug, but yields remained low.[30] In 1941, Florey and Heatley travelled to the US in order to interest pharmaceutical companies in producing the drug and inform them about their process.[30]
Florey and Chain shared the 1945 Nobel Prize in Medicine with Fleming for their work.
The challenge of mass-producing this drug was daunting. On March 14, 1942, the first patient was treated for streptococcal septicemia with US-made penicillin produced by Merck & Co.[32] Half of the total supply produced at the time was used on that one patient. By June 1942, just enough US penicillin was available to treat ten patients.[33] In July 1943, the War Production Board drew up a plan for the mass distribution of penicillin stocks to Allied troops fighting in Europe.[34] The results of fermentation research on corn steep liquor at the Northern Regional Research Laboratory at Peoria, Illinois, allowed the United States to produce 2.3 million doses in time for the invasion of Normandy in the spring of 1944. After a worldwide search in 1943, a mouldy cantaloupe in a Peoria, Illinois market was found to contain the best strain of mould for production using the corn steep liquor process.[35] Pfizer scientist Jasper H. Kane suggested using a deep-tank fermentation method for producing large quantities of pharmaceutical-grade penicillin.[36][37] Large-scale production resulted from the development of a deep-tank fermentation plant by chemical engineer Margaret Hutchinson Rousseau.[38] As a direct result of the war and the War Production Board, by June 1945, over 646 billion units per year were being produced.[34]
Penicillin was being mass-produced in 1944.
G. Raymond Rettew made a significant contribution to the American war effort by his techniques to produce commercial quantities of penicillin.[39] During World War II, penicillin made a major difference in the number of deaths and amputations caused by infected wounds among Allied forces, saving an estimated 12%–15% of lives.[citation needed] Availability was severely limited, however, by the difficulty of manufacturing large quantities of penicillin and by the rapid renal clearance of the drug, necessitating frequent dosing. Methods for mass production of penicillin were patented by Andrew Jackson Moyer in 1945.[40][41][42] Florey had not patented penicillin, having been advised by Sir Henry Dale that doing so would be unethical.[30]
Penicillin is actively excreted, and about 80% of a penicillin dose is cleared from the body within three to four hours of administration. Indeed, during the early penicillin era, the drug was so scarce and so highly valued that it became common to collect the urine from patients being treated, so that the penicillin in the urine could be isolated and reused.[43] This was not a satisfactory solution, so researchers looked for a way to slow penicillin excretion. They hoped to find a molecule that could compete with penicillin for the organic acid transporter responsible for excretion, such that the transporter would preferentially excrete the competing molecule and the penicillin would be retained. The uricosuric agent probenecid proved to be suitable. When probenecid and penicillin are administered together, probenecid competitively inhibits the excretion of penicillin, increasing penicillin's concentration and prolonging its activity. Eventually, the advent of mass-production techniques and semi-synthetic penicillins resolved the supply issues, so this use of probenecid declined.[43] Probenecid is still useful, however, for certain infections requiring particularly high concentrations of penicillins.[11][needs update]
After World War II, Australia was the first country to make the drug available for civilian use. In the U.S., penicillin was made available to the general public on March 15, 1945.[44]
Dorothy Hodgkin determined the chemical structure of penicillin.
Structure determination and total synthesis[edit]
Dorothy Hodgkin's model of penicillin's structure.
The chemical structure of penicillin was first proposed by Edward Abraham in 1942[26] and was later confirmed in 1945 using X-ray crystallography by Dorothy Crowfoot Hodgkin, who was also working at Oxford.[45] She later received the Nobel prize for this and other structure determinations.
Chemist John C. Sheehan at the Massachusetts Institute of Technology (MIT) completed the first chemical synthesis of penicillin in 1957.[46][47][48] Sheehan had started his studies into penicillin synthesis in 1948, and during these investigations developed new methods for the synthesis of peptides, as well as new protecting groups—groups that mask the reactivity of certain functional groups.[48][49] Although the initial synthesis developed by Sheehan was not appropriate for mass production of penicillins, one of the intermediate compounds in Sheehan's synthesis was 6-aminopenicillanic acid (6-APA), the nucleus of penicillin.[48][50][51][page needed] Attaching different groups to the 6-APA 'nucleus' of penicillin allowed the creation of new forms of penicillin.
Developments from penicillin[edit]
The narrow range of treatable diseases or "spectrum of activity" of the penicillins, along with the poor activity of the orally active phenoxymethylpenicillin, led to the search for derivatives of penicillin that could treat a wider range of infections. The isolation of 6-APA, the nucleus of penicillin, allowed for the preparation of semisynthetic penicillins, with various improvements over benzylpenicillin (bioavailability, spectrum, stability, tolerance).
The first major development was ampicillin in 1961. It offered a broader spectrum of activity than either of the original penicillins. Further development yielded β-lactamase-resistant penicillins, including flucloxacillin, dicloxacillin, and methicillin. These were significant for their activity against β-lactamase-producing bacterial species, but were ineffective against the methicillin-resistant Staphylococcus aureus (MRSA) strains that subsequently emerged.[citation needed]
Another development of the line of true penicillins was the antipseudomonal penicillins, such as carbenicillin, ticarcillin, and piperacillin, useful for their activity against Gram-negative bacteria. However, the usefulness of the β-lactam ring was such that related antibiotics, including the mecillinams, the carbapenems and, most important, the cephalosporins, still retain it at the center of their structures.[52]
Production[edit]
A 1957 fermentor (bioreactor) used to grow Penicillium mould.
Penicillin is a secondary metabolite of certain species of Penicillium and is produced when growth of the fungus is inhibited by stress. It is not produced during active growth. Production is also limited by feedback in the synthesis pathway of penicillin.[citation needed]
α-ketoglutarate + AcCoA → homocitrate → L-α-aminoadipic acid → L-lysine + β-lactam
The by-product, l-lysine, inhibits the production of homocitrate, so the presence of exogenous lysine should be avoided in penicillin production.
The Penicillium cells are grown using a technique called fed-batch culture, in which the cells are constantly subject to stress, which is required for induction of penicillin production. The available carbon sources are also important: Glucose inhibits penicillin production, whereas lactose does not. The pH and the levels of nitrogen, lysine, phosphate, and oxygen of the batches must also be carefully controlled.[citation needed]
The biotechnological method of directed evolution has been applied to produce by mutation a large number of Penicillium strains. These techniques include error-prone PCR, DNA shuffling, ITCHY, and strand-overlap PCR.
Semisynthetic penicillins are prepared starting from the penicillin nucleus 6-APA.
Biosynthesis[edit]
Penicillin G biosynthesis
Overall, there are three main and important steps to the biosynthesis of penicillin G (benzylpenicillin).
The first step is the condensation of three amino acids—L-α-aminoadipic acid, L-cysteine, L-valine into a tripeptide.[53][54][55] Before condensing into the tripeptide, the amino acid L-valine must undergo epimerization to become D-valine.[56][57] The condensed tripeptide is named δ-(L-α-aminoadipyl)-L-cysteine-D-valine (ACV). The condensation reaction and epimerization are both catalyzed by the enzyme δ-(L-α-aminoadipyl)-L-cysteine-D-valine synthetase (ACVS), a nonribosomal peptide synthetase or NRPS.
The second step in the biosynthesis of penicillin G is the oxidative conversion of linear ACV into the bicyclic intermediate isopenicillin N by isopenicillin N synthase (IPNS), which is encoded by the gene pcbC.[53][54] Isopenicillin N is a very weak intermediate, because it does not show strong antibiotic activity.[56]
The final step is a transamidation by isopenicillin N N-acyltransferase, in which the α-aminoadipyl side-chain of isopenicillin N is removed and exchanged for a phenylacetyl side-chain. This reaction is encoded by the gene penDE, which is unique in the process of obtaining penicillins.[53]
Members[edit]
Names
Method of administration
Notes
Penicillin G, benzylpenicillin IV or IM It has high urinary excretion and is produced as a salt of potassium or sodium.
Penicillin V, phenoxymethylpenicillin By mouth It is less active than benzylpenicillin against Gram-negative bacteria.
Benzathine benzylpenicillin, benzathine penicillin G IM Benzathine is a stabilizer that causes slower release over two to four weeks.
Procaine benzylpenicillin, penicillin G procaine IM Slow release.
Natural penicillins[edit]
Penicillin G
Penicillin K
Penicillin N
Penicillin O
Penicillin V
β-lactamase-resistant[edit]
Methicillin
Nafcillin
Oxacillin
Cloxacillin
Dicloxacillin
Flucloxacillin
Aminopenicillins[edit]
Ampicillin
Amoxicillin
Pivampicillin
Hetacillin
Bacampicillin
Metampicillin
Talampicillin
Epicillin
Carboxypenicillins[edit]
Carbenicillin
Ticarcillin
Temocillin
Ureidopenicillins[edit]
Mezlocillin
Piperacillin
β-lactamase inhibitors[edit]
Clavulanic acid
Sulbactam
Tazobactam
See also[edit]
Medicinal fungi
Penicillinase
Notes[edit]
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Jump up ^ Sheehan, John C.; Henery-Logan, Kenneth R. (June 20, 1959). "The Total Synthesis of Penicillin V". Journal of the American Chemical Society. 81 (12): 3089–3094. doi:10.1021/ja01521a044.
^ Jump up to: a b c E. J. Corey; John D. Roberts. "Biographical Memoirs: John Clark Sheehan". The National Academy Press. Retrieved January 28, 2013.
Jump up ^ Nicolaou, K.C.; Vourloumis, Dionisios; Winssinger, Nicolas; Baran, Phil S. (2000). "The Art and Science of Total Synthesis at the Dawn of the Twenty-First Century". Angewandte Chemie International Edition. 39 (1): 44–122. doi:10.1002/(SICI)1521-3773(20000103)39:1<44::AID-ANIE44>3.0.CO;2-L. PMID 10649349.
Jump up ^ "Professor John C. Sheehan Dies at 76". MIT News. April 1, 1992. Retrieved January 28, 2013.
Jump up ^ Sheehan, John C. (1982). The Enchanted Ring: The Untold Story of Penicillin. MIT Press. ISBN 978-0-262-19204-0.
Jump up ^ James, PharmD, Christopher W.; Cheryle Gurk-Turner, RPh (January 2001). "Cross-reactivity of beta-lactam antibiotics". Baylor University Medical Center Proceedings. Dallas, Texas: Baylor University Medical Center. 14 (1): 106–7. PMC 1291320  . PMID 16369597.
^ Jump up to: a b c Al-Abdallah, Q., Brakhage, A. A., Gehrke, A., Plattner, H., Sprote, P., Tuncher, A. (2004). "Regulation of Penicillin Biosynthesis in Filamentous Fungi". In Brakhage AA. Molecular Biotechnolgy of Fungal beta-Lactam Antibiotics and Related Peptide Synthetases. pp. 45–90. doi:10.1007/b99257. ISBN 3-540-22032-1. CS1 maint: Multiple names: authors list (link)
^ Jump up to: a b Brakhage, A. A. (1998). "Molecular Regulation of β-Lactam Biosynthesis in Filamentous Fungi". Microbiol Mol Biol Rev. 62 (3): 547–85. PMC 98925  . PMID 9729600.
Jump up ^ Baldwin, J. E., Byford, M. F., Clifton, I., Hajdu, J., Hensgens, C., Roach, P, Schofield, C. J.; Baldwin; Byford; Clifton; Hajdu; Hensgens; Roach (1997). "Proteins of the Penicillin Biosynthesis Pathway". Current Opinion in Structural Biology. 7 (6): 857–64. doi:10.1016/s0959-440x(97)80158-3. PMID 9434907. CS1 maint: Multiple names: authors list (link)
^ Jump up to: a b Fernandez, F. J., Fierro, F., Gutierrez, S, Kosalkova, K . Marcos, A. T., Martin, J. F., Velasco, J.; Gutiérrez; Fernández; Velasco; Fierro; Marcos; Kosalkova (September 1994). "Expression of Genes and Processing of Enzymes for the Biosynthesis of Penicillins and Cephalosporms". Antonie van Leeuwenhoek. 65 (3): 227–43. doi:10.1007/BF00871951. PMID 7847890. CS1 maint: Multiple names: authors list (link)
Jump up ^ Baker, W. L., Lonergan, G. T. "Chemistry of Some Fluorescamine-Amine Derivatives with Relevance to the Biosynthesis of Benzylpenicillin by Fermentation". J Chem Technol Biot. 2002, 77, pp1283-1288.
References[edit]
Nicolaou, K.C.; E.J. Corey (1996). Classics in Total Synthesis : Targets, Strategies, Methods (5. repr. ed.). Weinheim: VCH. ISBN 3-527-29284-5.
Dürckheimer, Walter; Blumbach, Jürgen; Lattrell, Rudolf; Scheunemann, Karl Heinz (March 1, 1985). "Recent Developments in the Field of β-Lactam Antibiotics". Angewandte Chemie International Edition in English. 24 (3): 180–202. doi:10.1002/anie.198501801.
Hamed, Refaat B.; Gomez-Castellanos, J. Ruben; Henry, Luc; Ducho, Christian; McDonough, Michael A.; Schofield, Christopher J. (January 1, 2013). "The enzymes of β-lactam biosynthesis". Natural Product Reports. 30 (1): 21–107. doi:10.1039/c2np20065a. PMID 23135477.
External links[edit]
Wikimedia Commons has media related to Penicillin antibiotics.
Model of Structure of Penicillin, by Dorothy Hodgkin et al., Museum of the History of Science, Oxford
The Discovery of Penicillin, A government produced film about the discovery of Penicillin by Sir Alexander Fleming, and the continuing development of its use as an antibiotic by Howard Florey and Ernst Boris Chain on YouTube.
Penicillin at The Periodic Table of Videos (University of Nottingham)
Penicillin Released to Civilians Will Cost $35 Per Patient Popular Science, August 1944, article at bottom of page
[show]
v
t
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Antibiotics active on the cell wall and envelope (J01C-J01D)
Intracellular
Inhibit peptidoglycan subunit synthesis and transport: NAM synthesis inhibition (Fosfomycin)
DADAL/AR inhibitors (Cycloserine)
bactoprenol inhibitors (Bacitracin)
Glycopeptide
Inhibit PG chain elongation: Vancomycin# (Oritavancin
Telavancin)
Teicoplanin (Dalbavancin)
Ramoplanin
β-lactams/
(inhibit PBP
cross-links)
Penicillins
(Penams)
Narrow
spectrum
β-lactamase sensitive
(1st generation)
Benzylpenicillin (G)#
Benzathine benzylpenicillin#
Procaine benzylpenicillin#
Phenoxymethylpenicillin (V)#
Propicillin‡
Pheneticillin‡
Azidocillin‡
Clometocillin‡
Penamecillin‡
β-lactamase resistant
(2nd generation)
Cloxacillin# (Dicloxacillin
Flucloxacillin)
Oxacillin
Nafcillin
Methicillin‡
Extended
spectrum
Aminopenicillins (3rd generation)
Amoxicillin#
Ampicillin# (Pivampicillin
Hetacillin‡
Bacampicillin‡
Metampicillin‡
Talampicillin‡)
Epicillin‡
Carboxypenicillins (4th generation)
Ticarcillin
Carbenicillin‡ / Carindacillin‡
Temocillin‡
Ureidopenicillins (4th generation)
Piperacillin
Azlocillin‡
Mezlocillin‡
Other
Mecillinam‡ (Pivmecillinam‡)
Sulbenicillin‡
Penems
Faropenem‡
Ritipenem§
Carbapenems
Ertapenem
Antipseudomonal (Doripenem
Imipenem
Meropenem)
Biapenem‡
Panipenem‡
Cephalosporins
/ Cephamycins
(Cephems)
1st generation
Cefazolin#
Cefalexin #
Cefadroxil
Cefapirin
Cefazedone‡
Cefazaflur‡
Cefradine‡
Cefroxadine‡
Ceftezole‡
Cefaloglycin‡
Cefacetrile‡
Cefalonium‡
Cefaloridine‡
Cefalotin‡
Cefatrizine‡
2nd generation
Cefaclor
Cefotetan
Cephamycin (Cefoxitin
Cefprozil
Cefuroxime
Cefuroxime axetil
Cefamandole‡
Cefminox‡
Cefonicid‡
Ceforanide‡
Cefotiam‡
Cefbuperazone‡
Cefuzonam‡
Cefmetazole)‡
Carbacephem‡ (Loracarbef‡)
3rd generation
Cefixime#
Ceftriaxone#
Antipseudomonal (Ceftazidime#
Cefoperazone)
Cefdinir
Cefcapene
Cefdaloxime
Ceftizoxime
Cefmenoxime
Cefotaxime#
Cefpiramide
Cefpodoxime
Ceftibuten
Cefditoren
Cefetamet‡
Cefodizime‡
Cefpimizole‡
Cefsulodin‡
Cefteram‡
Ceftiolene‡
Oxacephem (Flomoxef‡
Latamoxef‡)
4th generation
Cefepime
Cefozopran‡
Cefpirome‡
Cefquinome‡
5th generation
Ceftaroline fosamil
Ceftolozane
Ceftobiprole
Veterinary
Ceftiofur
Cefquinome
Cefovecin
Monobactams
Aztreonam
Tigemonam‡
Carumonam‡
Nocardicin A‡
β-lactamase inhibitors
Penam (Sulbactam
Tazobactam)
Clavam (Clavulanic acid)
Avibactam
Vaborbactam†
Combinations
Amoxicillin/clavulanic acid#
Imipenem/cilastatin#
Ampicillin/flucloxacillin
Ampicillin/sulbactam (Sultamicillin)
Ceftazidime/avibactam
Piperacillin/tazobactam
Ceftolozane/tazobactam
Other
polymyxins/detergent
Colistin
Polymyxin B
depolarizing
Daptomycin
Hydrolyze NAM-NAG
lysozyme
Tyrothricin
Gramicidin
Tyrocidine
Isoniazid#
Teixobactin
#WHO-EM
‡Withdrawn from market
Clinical trials:
†Phase III
§Never to phase III
[show]
v
t
e
GABA receptor modulators
Ionotropic
GABAA
Agonists: (+)-Catechin
Bamaluzole
Barbiturates (e.g., phenobarbital)
BL-1020
DAVA
Dihydromuscimol
GABA
Gabamide
GABOB
Gaboxadol (THIP)
Homotaurine (tramiprosate, 3-APS)
Ibotenic acid
iso-THAZ
iso-THIP
Isoguvacine
Isomuscimol
Isonipecotic acid
Kojic amine
Lignans (e.g., honokiol)
Methylglyoxal
Monastrol
Muscimol
Nefiracetam
Neuroactive steroids (e.g., allopregnanolone)
Org 20599
Phenibut
Picamilon
P4S
Progabide
Propofol
Quisqualamine
SL-75102
TACA
TAMP
Terpenoids (e.g., borneol)
Thiomuscimol
Tolgabide
ZAPA
Positive modulators (abridged; see here for a full list): α-EMTBL
Alcohols (e.g., ethanol)
Anabolic steroids
Avermectins (e.g., ivermectin)
Barbiturates (e.g., phenobarbital)
Benzodiazepines (e.g., diazepam)
Bromide compounds (e.g., potassium bromide)
Carbamates (e.g., meprobamate)
Carbamazepine
Chloralose
Chlormezanone
Clomethiazole
Dihydroergolines (e.g., ergoloid (dihydroergotoxine))
Etazepine
Etifoxine
Fenamates (e.g., mefenamic acid)
Flavonoids (e.g., apigenin, hispidulin)
Fluoxetine
Flupirtine
Imidazoles (e.g., etomidate)
Kava constituents (e.g., kavain)
Lanthanum
Loreclezole
Monastrol
Neuroactive steroids (e.g., allopregnanolone, cholesterol)
Niacin
Nicotinamide (niacinamide)
Nonbenzodiazepines (e.g., β-carbolines (e.g., abecarnil), cyclopyrrolones (e.g., zopiclone), imidazopyridines (e.g., zolpidem), pyrazolopyrimidines (e.g., zaleplon))
Norfluoxetine
Petrichloral
Phenols (e.g., propofol)
Phenytoin
Piperidinediones (e.g., glutethimide)
Propanidid
Pyrazolopyridines (e.g., etazolate)
Quinazolinones (e.g., methaqualone)
Retigabine (ezogabine)
ROD-188
Skullcap constituents (e.g., baicalin)
Stiripentol
Sulfonylalkanes (e.g., sulfonmethane (sulfonal))
Topiramate
Valerian constituents (e.g., valerenic acid)
Volatiles/gases (e.g., chloral hydrate, chloroform, diethyl ether, paraldehyde, sevoflurane)
Antagonists: Bicuculline
Coriamyrtin
Dihydrosecurinine
Gabazine (SR-95531)
Hydrastine
Hyenachin (mellitoxin)
PHP-501
Pitrazepin
Securinine
Sinomenine
SR-42641
SR-95103
Thiocolchicoside
Tutin
Negative modulators: 1,3M1B
3M2B
11-Ketoprogesterone
17-Phenylandrostenol
α5IA (LS-193,268)
β-CCB
β-CCE
β-CCM
β-CCP
β-EMGBL
Anabolic steroids
Amiloride
Anisatin
β-Lactams (e.g., penicillins, cephalosporins, carbapenems)
Basmisanil
Bemegride
Bilobalide
CHEB
Cicutoxin
Cloflubicyne
Cyclothiazide
DHEA
DHEA-S
Dieldrin
(+)-DMBB
DMCM
DMPC
EBOB
Etbicyphat
FG-7142 (ZK-31906)
Fiproles (e.g., fipronil)
Flavonoids (e.g., amentoflavone, oroxylin A)
Flumazenil
Fluoroquinolones (e.g., ciprofloxacin)
Flurothyl
Furosemide
Iomazenil (123I)
Isoallopregnanolone
Isopregnanolone (sepranolone)
L-655,708
Laudanosine
Leptazol
Lindane
MaxiPost
Morphine
Morphine-3-glucuronide
MRK-016
Naloxone
Naltrexone
Nicardipine
Nonsteroidal antiandrogens (e.g., apalutamide, bicalutamide, enzalutamide, flutamide, nilutamide)
Oenanthotoxin
Pentylenetetrazol (pentetrazol)
Phenylsilatrane
Picrotoxin (i.e., picrotin and picrotoxinin)
Pregnenolone sulfate
Propybicyphat
PWZ-029
Radequinil
Ro 15-4513
Ro 19-4603
RO4882224
RO4938581
Sarmazenil
SCS
Suritozole
TB-21007
TBOB
TBPS
TCS-1105
Terbequinil
TETS
Thujone
U-93631
Zinc
ZK-93426
GABAA-ρ
Agonists: BL-1020
CACA
CAMP
Homohypotaurine
GABA
GABOB
Ibotenic acid
Isoguvacine
Muscimol
N4-Chloroacetylcytosine arabinoside
Picamilon
Progabide
TACA
TAMP
Thiomuscimol
Tolgabide
Positive modulators: Allopregnanolone
Alphaxolone
ATHDOC
Lanthanides
Antagonists: (S)-2-MeGABA
(S)-4-ACPBPA
(S)-4-ACPCA
2-MeTACA
3-APMPA
4-ACPAM
4-GBA
cis-3-ACPBPA
CGP-36742 (SGS-742)
DAVA
Gabazine (SR-95531)
Gaboxadol (THIP)
I4AA
Isonipecotic acid
Loreclezole
P4MPA
P4S
SKF-97541
SR-95318
SR-95813
TPMPA
trans-3-ACPBPA
ZAPA
Negative modulators: 5α-Dihydroprogesterone
Bilobalide
Loreclezole
Picrotoxin (picrotin, picrotoxinin)
Pregnanolone
ROD-188
THDOC
Zinc
Metabotropic
GABAB
Agonists: 1,4-Butanediol
4-Fluorophenibut
Aceburic acid
Arbaclofen
Arbaclofen placarbil
Baclofen
BL-1020
GABA
Gabamide
GABOB
GBL
GHB
GHBAL
GHV
GVL
Isovaline
Lesogaberan
Phenibut
Picamilon
Progabide
Sodium oxybate
SKF-97,541
SL 75102
Tolgabide
Tolibut
Positive modulators: ADX-71441
BHF-177
BHFF
BSPP
CGP-7930
CGP-13501
GS-39783
rac-BHFF
KK-92A
Antagonists: 2-Hydroxysaclofen
CGP-35348
CGP-46381
CGP-52432
CGP-54626
CGP-55845
CGP-64213
DAVA
Homotaurine (tramiprosate, 3-APS)
Phaclofen
Saclofen
SCH-50911
SKF-97541
Negative modulators: Compound 14
See also
Receptor/signaling modulators
GABAA receptor positive modulators
GABA metabolism/transport modulators
Authority control
GND: 4045094-6
NDL: 00569084
Retrieved from "https://en.wikipedia.org/w/index.php?title=Penicillin&oldid=819104917"
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Teddy Altman
From Wikipedia, the free encyclopedia
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For the Marvel Comics character, see Hulkling.
This television-related article describes a work or element of fiction in a primarily in-universe style. Please help rewrite it to explain the fiction more clearly and provide non-fictional perspective. (June 2010) (Learn how and when to remove this template message)
Teddy Altman
Grey's Anatomy character
Kim Raver as Dr. Teddy Altman in 2010.
First appearance
"New History" (6.09)
November 12, 2009
(as recurring cast)
"Sympathy for the Parents" (6.19)
April 1, 2010
(as series regular)
Last appearance
"Flight" (8.24)
May 17, 2012
(as series regular)
Created by
Shonda Rhimes
Portrayed by
Kim Raver
Information
Occupation
Attending cardiothoracic surgeon at Seattle Grace Mercy West Hospital (former)
Title
Chief of Cardiothoracic Surgery
M.D.
F.A.C.S.
Spouse(s)
Henry Burton (deceased)
Significant other(s)
Andrew Perkins
Mark Sloan
Theodora "Teddy" Altman, M.D. is a fictional character from the ABC medical drama Grey's Anatomy, portrayed by actress Kim Raver. She was an attending cardiothoracic surgeon at Seattle Grace Mercy West Hospital, the fictional institution where the show is set. She leaves the show in the 8th-season finale after it is revealed that she has been offered a chief position with Army Medical Command, but has turned it down out of loyalty to Dr. Owen Hunt. In order to liberate her from the hospital where her husband died, Hunt fires her from Seattle Grace. Teddy returns for a few episodes in season 14.
Contents
[hide]
1 Storylines
2 Development
2.1 Casting and creation
2.2 Characterization
3 Reception
4 References
5 External links
Storylines[edit]
Teddy attended the University of Texas Southwestern Medical Center. She completed her surgical residency at George Washington University Medical School and her fellowship at the Mayo Clinic in Florida. As an attending physician, Teddy worked at Columbia, but after her best friend was killed during the collapse of the second tower on September 11, 2001, she left and joined the army, meeting trauma surgeon Owen Hunt (Kevin McKidd) during her tour in Baghdad.
Owen brings Teddy to Seattle Grace Mercy West hospital to mentor his girlfriend, Cristina Yang (Sandra Oh). Teddy admits that she is in love with Owen, but he tells her that he loves Cristina. When Teddy assigns Cristina a difficult surgery for her first solo cardiothoracic case and refuses to assist, Owen questions Teddy's motives. Teddy decides to leave Seattle Grace; Cristina pleads with her to stay, even offering to break up with Owen if Teddy will continue to teach her. Although Teddy agrees to stay, Owen convinces Cristina to stay with him, and Teddy briefly removes her from her service.
Teddy develops a friendship with pediatric surgeon Arizona Robbins (Jessica Capshaw), who sets her up with plastic surgeon Mark Sloan (Eric Dane). They have a brief relationship, which they both enjoy despite knowing that neither wants the other—Teddy still wants Owen, and Mark is in love with Lexie Grey (Chyler Leigh). The two separate amicably when Teddy walks in on Mark sleeping with resident Reed Adamson (Nora Zehetner).
Towards the end of season six, Teddy has to fight for her job as Chief of Cardiothoracic Surgery. Cristina asks Owen to put in a good word for Teddy; he does the opposite by telling Chief of Surgery Derek Shepherd (Patrick Dempsey) that she would land on her feet. Ultimately another candidate refuses to take the post and Teddy receives a full-time contract. Teddy later learns of, and is hurt by Owen's betrayal.
Teddy has a brief relationship with Dr. Andrew Perkins, whose service at the hospital is temporary. Before his departure, he suggests that Teddy has a tendency to fall for people who are either otherwise engaged or only in town for a month. She later meets Henry Burton, a patient with the rare genetic condition Von Hippel-Lindau disease, who can no longer afford to pay for his medical care. Teddy marries him so that he can use her health insurance, and only comes to appreciate the gravity of this decision when Henry suffers a near fatal complication of his illness. Teddy discovers that he has listed her as his emergency contact and is forced to make a life-or-death decision regarding his care, not as his doctor but as his wife. Though the newly-weds both maintain that theirs is a simple marriage of convenience, and Teddy continues to date other men, Henry later confesses that he has feelings for Teddy. She tells him she does not feel the same way.
Teddy again removes Cristina from her service when she performs a surgery despite Teddy's opposition. She tells Owen that Cristina's over-abundance of confidence makes her dangerous, and that she will keep Cristina off her service until she feels she is ready to return. When Andrew returns and asks Teddy to move to Germany with him, she accepts, and agrees to divorce Henry. However, in the seventh season finale, Teddy changes her mind and tells Henry that she is falling in love with him. The two begin their married life properly, but in season eight, Henry dies, leaving Teddy distraught. She blames Owen because she wasn't told that Henry had died until after her surgery on another patient. Feeling that he put the hospital before her, she breaks off her friendship with him, causing problems with them being able to work together that are later made worse by Cristina's own relationship troubles with Owen (During this time, Cristina tells Owen that he has to grant Teddy her anger, to which an enraged Owen lashes out the hypocrisy in the situation, given that when Cristina discovered she was pregnant with Owen's child, she told him that keeping the pregnancy was non negotiable and wanted to pursue an abortion, despite Owen's desire to have a child, and his pleas to keep the pregnancy, points out that Cristina never "granted him any anger" over what he thought was her selfish decision). After a particularly bad case, Dr. Bailey sternly tells Teddy that what happened with Henry was not Owen's fault and that Teddy knows this and needs to get over it, which pushes Teddy to behave more civilly towards Owen, but she finally lets go of her anger after she desperately begs Owen to convince Cristina (who by this point has broken up with him) to not transfer away from Seattle and is left shocked and silent when Owen furiously tells her he will not do that because he and Teddy are only co-workers and, as she made very clear, not friends and therefore she has no right to ask him for any help or favors. She and Owen eventually make up in the season finale. Owen finds out she was offered a job at the United States Army Medical Command, but turned it down because she wanted to be there for Owen, if he and Cristina were to separate. He ultimately fires her and she does take the military job, and tells her that he'll be okay as they part having restored their friendship.Teddy and Owen make up and hug each other goodbye as he wants her to take the job offer, which would be good for her.
Teddy was later mentioned in season thirteen episode "True Colors." Army officers knocked at Owen's door stating that his sister Megan is believed to have been found alive ten years after her disappearance. At first, Owen is not sure what to believe, but his wife Amelia Shepherd mentioned to Owen that Teddy saw Megan and recognized her. This seemed to be the first time Teddy was mentioned after her departure.
Development[edit]
Raver initially signed for a recurring role, but was promoted to a series regular.
Casting and creation[edit]
In October 2009, it was reported that actress Kim Raver would play the character and have a recurring role on the show's sixth season.[1] In January 2010, Raver was promoted to a series regular.[2]
On May 18, 2012, the day after the season eight finale, Grey's Anatomy creator, Shonda Rhimes, announced that it was Raver's decision to leave the show, "I know this season’s finale had some surprises for viewers and the exit of Kim Raver was one of the big ones. But Kim’s series option was up and she was ready to give Teddy Altman a much-needed vacation. It’s been a pleasure working with someone as talented and funny and kind as Kim; everyone is going to miss her terribly. I like to imagine that Teddy is still out there in the Grey’s Anatomy universe, running Army Medical Command and building a new life."[3] When the news of the character's departure was released, Raver wrote on her Twitter, "I've had one of the best times of my creative career working on Grey's with Shonda, Betsy and the best cast on Television," she wrote, adding: "I feel fortunate and grateful to have worked with such an amazing team at GA [Grey's Anatomy]. [I] am going to miss everyone!! And to the GA [Grey's Anatomy] fans, you guys rock! I am sure S9 [season nine] will be great!"[4] On June 20, 2017, it was announced that Raver would be reprising her role as Teddy Altman for a guest arc during the show's 14th season.[5]
Characterization[edit]
This section is empty. You can help by adding to it. (July 2012)
We see Teddy as a person who is willing to do whatever possible to make herself a much appreciated doctor and friend at Grey Sloan. In Season 14's premiere, "Break Down the House", Teddy and Owen Reunite after long times away from each other. Teddy comforts Owen after he is on the verge of having a meltdown. is this just the beginning of a newly discovered friendship between the two after so much time away from each other?
Reception[edit]
This section needs expansion. You can help by adding to it. (July 2012)
Entertainment Weekly writer Tanner Stransky found Altman had not been given a good storyline until the arrival of Henry: "I think Kim Raver has always been rather under-used on this show, until more recently."[6]
References[edit]
Specific
Jump up ^ 'Grey's Anatomy' scoop: Kim Raver to play spoiler in Owen-Cristina romance
Jump up ^ Kim Raver becomes series regular on 'Grey's Anatomy'
Jump up ^ 'Grey's Anatomy' season finale: Boss explains two shocking exits
Jump up ^ Eggenberger, Nicole. "Chyler Leigh, Kim Raver Leave Grey's Anatomy". US Weekly. Celebrity News. Retrieved May 18, 2012.
Jump up ^ Andreeva, Nellie. "'Grey's Anatomy': Kim Raver To Make A Return In Season 14". Deadline. Retrieved June 20, 2017.
Jump up ^ Stransky, Tanner (November 10, 2011). "'Grey's Anatomy' recap: Death and Devastation". Entertainment Weekly. Time Inc. p. 2. Retrieved July 29, 2012.
General
"Grey's Anatomy: Episode Recap Guide". ABC. Retrieved June 19, 2012.
External links[edit]
Grey's Anatomy portal
Fictional characters portal
Teddy Altman at ABC.com
Teddy Altman on IMDb
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