Abstract
Synthetic modifications have been made directly to the cyclic peptide core of polymyxin B, enabling the further understanding of structure activity relationships of this antimicrobial peptide. Such modified polymyxins are also substrates for enzymic hydrolysis, enabling the synthesis of a variety of semi-synthetic analogues, resulting in compounds with increased in vitro antibacterial activity.
Keywords:
Antibiotics; Drug resistance; Gram negative; Peptides; Polymyxins.
Copyright © 2020 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Anti-Bacterial Agents / chemical synthesis
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Anti-Bacterial Agents / chemistry*
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Anti-Bacterial Agents / pharmacology
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Cell Line
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Cell Survival / drug effects
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Escherichia coli / drug effects
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Humans
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Hydrolysis
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Microbial Sensitivity Tests
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Peptides, Cyclic / chemistry
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Polymyxin B / chemical synthesis
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Polymyxin B / chemistry*
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Polymyxin B / pharmacology
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Pseudomonas aeruginosa / drug effects
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Structure-Activity Relationship
Substances
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Anti-Bacterial Agents
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Peptides, Cyclic
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Polymyxin B