Invanz Sandbox: Difference between revisions
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== Function == | == Function == | ||
'''Function:''' Invanz is used to treat a range of bacterial infections caused by Gram positive and Gram negative bacteria as well as a range of both aerobic and anaerobic bacteria. Invanz works by inhibiting cell wall synthesis via binding to penicillin binding proteins (PBPs). Invanz is stable against hydrolysis from many beta-lactamases including penicillinases and cephalosporinases, but is unstable against metallo-beta-lactamases | '''Function:''' Invanz is used to treat a range of bacterial infections caused by Gram positive and Gram negative bacteria as well as a range of both aerobic and anaerobic bacteria. Invanz works by inhibiting cell wall synthesis via binding to penicillin binding proteins (PBPs). Invanz is stable against hydrolysis from many beta-lactamases including penicillinases and cephalosporinases, but is unstable against metallo-beta-lactamases <ref name="merck" />. Beta-lactamases are secreted by bacteria to provide resistance to antibiotics; however, Invanz is relatively unaffected by these beta-lactamases and thus is an effective treatment for various bacterial infections <ref>PMID: 25561890</ref>. The unique structural features of Invanz equip this drug with some of the widest spectrum and most potent antimicrobial activity of carbapenem antibiotics today <ref>PMID: 12951340</ref>. | ||
== Structural highlights == | == Structural highlights == | ||
'''Structure:''' Invanz is a carbapenem which is a beta-lactam antibiotic (contains a beta lactam ring) that has antimicrobial action via inhibition of cell wall synthesis. This class of antibiotics is known for its broad spectrum of activity, and its structure allows it to bind penicillin binding proteins (PBPs) to inhibit bacterial cell wall synthesis in a variety of bacterial types <ref>PMID: 17488146</ref><ref name="Invanz1">...</ref>. Antibiotic resistance to carbapenems largely results from ability of the bacterial species to secrete beta-lactamase enzymes that can degrade the antimicrobial. Invanz has resistance to many beta-lactamases since it has a trans-1-hydroxyethyl group | '''Structure:''' Invanz is a carbapenem which is a beta-lactam antibiotic (contains a beta lactam ring) that has antimicrobial action via inhibition of cell wall synthesis. This class of antibiotics is known for its broad spectrum of activity, and its structure allows it to bind penicillin binding proteins (PBPs) to inhibit bacterial cell wall synthesis in a variety of bacterial types <ref>PMID: 17488146</ref><ref name="Invanz1">...</ref>. Antibiotic resistance to carbapenems largely results from ability of the bacterial species to secrete beta-lactamase enzymes that can degrade the antimicrobial. Invanz has resistance to many beta-lactamases since it has a trans-1-hydroxyethyl group that confers resistance of the antibiotic to degradation by most beta-lactamases <ref>PMID: 15150178 </ref> <ref name="hammond">...</ref>. The beta lactam ring is a four-membered, nitrogen-containing ring that binds to PBPs, thus making them unable to continue bacterial cell wall synthesis. PBPs are enzymes found in the cell membrane that aid in cross-linking of peptidoglycan during cell wall synthesis <ref>PMID: 18266856</ref>. By inactivating PBPs and inhibiting cell wall synthesis, bacterial cell death will occur as the cells lyse due to osmotic pressure <ref>Page, M.L. The mechanisms of reactions of beta lactam antibiotics. Accounts of Chemical Research, 1984, 17(4), 144-151 DOI: 10.1021/ar00100a005</ref>. | ||
There are various structural features of Invanz that make make administration of the drug easy. Older carbapenems required patients to take a dehydropeptidase-1 (DHP-1) inhibitor since the DHAP enzyme found in the human renal system could interfere with the action of the carbapenem by degrading the antibiotic <ref name="Invanz1" />. Invanz is a unique antibiotic because it has a 1-beta-methyl substituent that shields the beta-lactam carbonyl from DHP-1 degradation <ref name="hammond">...</ref>. The meta-substituted benzoic acid substituent increases the molecular weight and makes the drug more soluble in nonpolar solvents. Additionally, the carboxylic acid substituent becomes ionized at physiological pH, so the ertapenem has a net negative charge. Increased solubility in non polar solvents and the net negative charge allows the drug to bind human plasma proteins with an extended half-life in the blood stream, and thus the drug only has to be administered once daily <ref name="hammond" />. Invanz largely travels in the bloodstream bound to the human plasma protein albumin <ref name="merck" />. | There are various structural features of Invanz that make make administration of the drug easy. Older carbapenems required patients to take a dehydropeptidase-1 (DHP-1) inhibitor since the DHAP enzyme found in the human renal system could interfere with the action of the carbapenem by degrading the antibiotic <ref name="Invanz1" />. Invanz is a unique antibiotic because it has a 1-beta-methyl substituent that shields the beta-lactam carbonyl from DHP-1 degradation <ref name="hammond">...</ref>. The meta-substituted benzoic acid substituent increases the molecular weight and makes the drug more soluble in nonpolar solvents. Additionally, the carboxylic acid substituent becomes ionized at physiological pH, so the ertapenem has a net negative charge. Increased solubility in non polar solvents and the net negative charge allows the drug to bind human plasma proteins with an extended half-life in the blood stream, and thus the drug only has to be administered once daily <ref name="hammond" />. Invanz largely travels in the bloodstream bound to the human plasma protein albumin <ref name="merck" />. | ||
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== References == | == References == | ||
<references /> | <references /> | ||
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