How B-lactam drugs work: Difference between revisions
Ann Taylor (talk | contribs) No edit summary |
No edit summary |
||
| (2 intermediate revisions by one other user not shown) | |||
| Line 1: | Line 1: | ||
==How beta-lactam drugs work== | ==How beta-lactam drugs work== | ||
<StructureSection load='1CEG' size='340' side='right' caption='transpeptidase' scene=''> | <StructureSection load='1CEG' size='340' side='right' caption='D-alanyl-D-alanine carboxipeptidase transpeptidase complex with cephalothin (PDB code [[1ceg]])' scene=''> | ||
Beta-lactam drugs are a classic way of treating bacterial infections. Since bacteria have cell walls and people don't, drugs that target cell wall synthesis should have fewer side effects. Beta-lactam drugs include penicillin, which was discovered by 1928 by Alexander Fleming. He observed that colonies of Penicillium mold growing in his bacterial cultures created zones where bacteria couldn't grow.<ref>PMID:26243971</ref> He then isolated the specific compound that was responsible for this effect, penicillin. The term "beta lactam" refers to the four membered ring structure that is found in this class of antibiotics. [[Image:DalaDala_vs_penicillin.png|left|300 px]] | Beta-lactam drugs are a classic way of treating bacterial infections. Since bacteria have cell walls and people don't, drugs that target cell wall synthesis should have fewer side effects. Beta-lactam drugs include penicillin, which was discovered by 1928 by Alexander Fleming. He observed that colonies of Penicillium mold growing in his bacterial cultures created zones where bacteria couldn't grow.<ref>PMID:26243971</ref> He then isolated the specific compound that was responsible for this effect, penicillin. The term "beta lactam" refers to the four membered ring structure that is found in this class of antibiotics. [[Image:DalaDala_vs_penicillin.png|left|300 px]] | ||
| Line 13: | Line 13: | ||
How do bacteria become resistant to penicillin and other beta lactam antibiotics? Some bacteria have an enzyme called penicillinase, which inactivates penicillin by cutting the beta lactam ring to form a carboxylic acid and an amine. This prevents the antibiotic from reacting with the serine residue in the transpeptidase, making it inactive. The gene for this enzyme is located on a bacterial plasmid, and can be transferred from one bacteria to another, causing antibacterial resistance to spread. | How do bacteria become resistant to penicillin and other beta lactam antibiotics? Some bacteria have an enzyme called penicillinase, which inactivates penicillin by cutting the beta lactam ring to form a carboxylic acid and an amine. This prevents the antibiotic from reacting with the serine residue in the transpeptidase, making it inactive. The gene for this enzyme is located on a bacterial plasmid, and can be transferred from one bacteria to another, causing antibacterial resistance to spread. | ||
For more information about penicillin binding proteins, please see the Molecule of the Month page for penicillin binding proteins. [https://pdb101.rcsb.org/motm/29] | For more information about penicillin binding proteins, please see the Molecule of the Month page for penicillin binding proteins. [https://pdb101.rcsb.org/motm/29] and [[Penicillin-binding protein]]. | ||
See also [[Beta-lactam antibiotics]] | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||