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PMID: 10828288 Published · ppublish English Journal Article Review

Inhibition of transglycosylation involved in bacterial peptidoglycan synthesis.

Current medicinal chemistry ·Vol. 7 ·No. 8 ·2000-08-00 ·Pages 801-20

Goldman RC, Gange D

Abstract

The continuing spectre of resistance to antimicrobial agents has driven a sustained search for new agents that possess activity on drug resistant bacteria. Although several paths are available to reach this goal, the most generalized would be the discovery and clinical development of an agent that acts on a new target which has not yet experienced selective pressure in the clinical setting. Such a target should be essential to the growth and survival of bacteria, and sufficiently different from, or better still non-existent in, the human host. The transglycosylation reaction that polymerizes biochemical intermediates into peptidoglycan qualifies as such a target. This biochemical system accepts the basic unit N-acetylglucosamine-beta-1, 4-N-acetyl-muramyl-pentapeptide-pyrophosphoryl-undecaprenol (lipid II), and leads to polymerization of the N-acetylglucosamine -beta-1, 4-N-acetyl-muramyl-pentapeptide segment into peptidoglycan. Approaches to targeting this reaction include modification of known glycolipid and glycopeptide natural product antibiotics. The synthesis and antibacterial activity of synthetic analogs of moenomycin having novel antibacterial activities not present in the parent structure will be presented, together with the combinatorial chemistry and assay systems leading to their discovery. Likewise, we will discuss chemical modifications to specific glycopeptide antibiotics that have extended their spectrum to include vancomycin resistant enterococci that substitute D-alanyl-D-lactate for D-alanyl-D-alanine in their peptidoglycan. Two differing theories, one positing the generation of high affinity, specific binding to D-alanyl-D-lactate via glycopeptide dimerization and/or membrane anchoring, and the other supporting direct targeting of the modified glycopeptide to the transglycosylation complex, seek to explain the mechanism of action on vancomycin resistant enterococci. Biochemical evidence in support of these two theories will be discussed.

MeSH Terms
Anti-Bacterial Agents/chemistry,pharmacology Bacterial Proteins Bambermycins/chemistry,metabolism,pharmacology Carrier Proteins/antagonists & inhibitors,metabolism Combinatorial Chemistry Techniques Glycosylation Gram-Positive Bacteria/drug effects,metabolism Hexosyltransferases Humans Molecular Structure Muramoylpentapeptide Carboxypeptidase/antagonists & inhibitors,metabolism Penicillin-Binding Proteins Peptidoglycan/biosynthesis,metabolism Peptidyl Transferases Vancomycin/analogs & derivatives,metabolism,pharmacology Vancomycin Resistance/physiology
Chemicals
Anti-Bacterial Agents Bacterial Proteins Carrier Proteins Penicillin-Binding Proteins Peptidoglycan Bambermycins Vancomycin Peptidyl Transferases Hexosyltransferases Muramoylpentapeptide Carboxypeptidase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Goldman R C
IRL Inc., 8 Cedar Brook Drive, Cranbury, NJ 08512, USA. rgoldman@irl.incara.com
Gange D
Article Info
Journal
Current medicinal chemistry
Abbr.
Curr Med Chem
ISSN
0929-8673
Published
2000-08-00
Pages
801-20
Language
English
Region
United Arab Emirates
NLM ID
9440157
Subset
IM
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