Semisynthetic Approaches to Laspartomycin Analogues

Laspartomycin C (1), a lipopeptide antibiotic related to amphomycin, consists of a cyclic peptide core and an aspartic acid unit external to the core and linking this to a C15-2,3-unsaturated fatty acid. This was reported initially to be active against Staphylococcus aureus, and more recent studies...

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Bibliographic Details
Published in:Journal of natural products (Washington, D.C.) D.C.), 2007-03, Vol.70 (3), p.447-450
Main Authors: Curran, William V, Leese, Richard A, Jarolmen, Howard, Borders, Donald B, Dugourd, Dominique, Chen, Yuchen, Cameron, Dale R
Format: Article
Language:English
Subjects:
Amidohydrolases - metabolism
Aminohydrolases - metabolism
Anti-Bacterial Agents - chemical synthesis
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacology
Antibacterial agents
Antibiotics. Antiinfectious agents. Antiparasitic agents
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Enterococcus faecalis - drug effects
Enterococcus faecium - drug effects
Fundamental and applied biological sciences. Psychology
Lipopeptides
Medical sciences
Methicillin Resistance - drug effects
Methods. Procedures. Technologies
Microbial Sensitivity Tests
Micromonosporaceae - enzymology
Molecular Structure
Oligopeptides - chemistry
Peptides, Cyclic - chemical synthesis
Peptides, Cyclic - chemistry
Peptides, Cyclic - pharmacology
Pharmacology. Drug treatments
Staphylococcus aureus - drug effects
Tryptophan - chemistry
Vancomycin Resistance - drug effects
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Summary:Laspartomycin C (1), a lipopeptide antibiotic related to amphomycin, consists of a cyclic peptide core and an aspartic acid unit external to the core and linking this to a C15-2,3-unsaturated fatty acid. This was reported initially to be active against Staphylococcus aureus, and more recent studies have shown that it is active against VRE, VISA, and MRSA isolates. The enzymatic cleavage of the fatty acid tail was accomplished with a deacylase produced by Actinoplanes utahensis and resulted in two peptides, designated Peptide 1 and Peptide 2. Semisynthetic derivatives of both peptides have been made, and the principal requirement for biological activity appears to be the presence of an acylaspartic acid.
ISSN:0163-3864
1520-6025
DOI:10.1021/np068062b