Synthesis and structure-activity relationship studies of N-terminal analogues of the antimicrobial peptide tridecaptin A(1)

Stephen A Cochrane; Christopher T Lohans; Jeremy R Brandelli; George Mulvey; Glen D Armstrong; John C Vederas

doi:10.1021/jm401779d

Synthesis and structure-activity relationship studies of N-terminal analogues of the antimicrobial peptide tridecaptin A(1)

Stephen A Cochrane, Christopher T Lohans, Jeremy R Brandelli, George Mulvey, Glen D Armstrong, John C Vederas

School of Chemistry and Chemical Engineering

Research output: Contribution to journal › Article › peer-review

37 Citations (Scopus)

Abstract

Chemical synthesis was used to increase the potency of the antimicrobial lipopeptide tridecaptin A1. Lipid tail modification proved to be an ideal platform for synthesizing structurally simpler analogues that are not readily accessible by isolation. The stereochemical elements of the tridecaptin A1 lipid tail are not essential for antimicrobial activity and could be replaced with hydrophobic aliphatic or aromatic groups. Some simpler analogues displayed potent antimicrobial activity against Gram-negative bacteria, including Campylobacter jejuni, Escherichia coli O157:H7, and multidrug resistant Klebsiella pneumoniae.

Original language	English
Pages (from-to)	1127-31
Journal	Journal of Medicinal Chemistry
Volume	57
Issue number	3
Early online date	30 Jan 2014
DOIs	https://doi.org/10.1021/jm401779d
Publication status	Published - 13 Feb 2014

Keywords

Anti-Bacterial Agents
Antimicrobial Cationic Peptides
Drug Resistance, Bacterial
Gram-Negative Bacteria
Hemolysis
Hydrophobic and Hydrophilic Interactions
Lipopeptides
Peptides
Stereoisomerism
Structure-Activity Relationship
Journal Article
Research Support, Non-U.S. Gov't

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Stephen Cochrane
- s.cochrane@qub.ac.uk
Person: Academic

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title = "Synthesis and structure-activity relationship studies of N-terminal analogues of the antimicrobial peptide tridecaptin A(1)",

abstract = "Chemical synthesis was used to increase the potency of the antimicrobial lipopeptide tridecaptin A1. Lipid tail modification proved to be an ideal platform for synthesizing structurally simpler analogues that are not readily accessible by isolation. The stereochemical elements of the tridecaptin A1 lipid tail are not essential for antimicrobial activity and could be replaced with hydrophobic aliphatic or aromatic groups. Some simpler analogues displayed potent antimicrobial activity against Gram-negative bacteria, including Campylobacter jejuni, Escherichia coli O157:H7, and multidrug resistant Klebsiella pneumoniae.",

keywords = "Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Drug Resistance, Bacterial, Gram-Negative Bacteria, Hemolysis, Hydrophobic and Hydrophilic Interactions, Lipopeptides, Peptides, Stereoisomerism, Structure-Activity Relationship, Journal Article, Research Support, Non-U.S. Gov't",

author = "Cochrane, {Stephen A} and Lohans, {Christopher T} and Brandelli, {Jeremy R} and George Mulvey and Armstrong, {Glen D} and Vederas, {John C}",

year = "2014",

month = feb,

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doi = "10.1021/jm401779d",

language = "English",

volume = "57",

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journal = "Journal of Medicinal Chemistry",

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Synthesis and structure-activity relationship studies of N-terminal analogues of the antimicrobial peptide tridecaptin A(1). / Cochrane, Stephen A; Lohans, Christopher T; Brandelli, Jeremy R; Mulvey, George; Armstrong, Glen D; Vederas, John C.

In: Journal of Medicinal Chemistry, Vol. 57, No. 3, 13.02.2014, p. 1127-31.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Synthesis and structure-activity relationship studies of N-terminal analogues of the antimicrobial peptide tridecaptin A(1)

AU - Cochrane, Stephen A

AU - Lohans, Christopher T

AU - Brandelli, Jeremy R

AU - Mulvey, George

AU - Armstrong, Glen D

AU - Vederas, John C

PY - 2014/2/13

Y1 - 2014/2/13

N2 - Chemical synthesis was used to increase the potency of the antimicrobial lipopeptide tridecaptin A1. Lipid tail modification proved to be an ideal platform for synthesizing structurally simpler analogues that are not readily accessible by isolation. The stereochemical elements of the tridecaptin A1 lipid tail are not essential for antimicrobial activity and could be replaced with hydrophobic aliphatic or aromatic groups. Some simpler analogues displayed potent antimicrobial activity against Gram-negative bacteria, including Campylobacter jejuni, Escherichia coli O157:H7, and multidrug resistant Klebsiella pneumoniae.

AB - Chemical synthesis was used to increase the potency of the antimicrobial lipopeptide tridecaptin A1. Lipid tail modification proved to be an ideal platform for synthesizing structurally simpler analogues that are not readily accessible by isolation. The stereochemical elements of the tridecaptin A1 lipid tail are not essential for antimicrobial activity and could be replaced with hydrophobic aliphatic or aromatic groups. Some simpler analogues displayed potent antimicrobial activity against Gram-negative bacteria, including Campylobacter jejuni, Escherichia coli O157:H7, and multidrug resistant Klebsiella pneumoniae.

KW - Anti-Bacterial Agents

KW - Antimicrobial Cationic Peptides

KW - Drug Resistance, Bacterial

KW - Gram-Negative Bacteria

KW - Hemolysis

KW - Hydrophobic and Hydrophilic Interactions

KW - Lipopeptides

KW - Peptides

KW - Stereoisomerism

KW - Structure-Activity Relationship

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1021/jm401779d

DO - 10.1021/jm401779d

M3 - Article

C2 - 24479847

VL - 57

SP - 1127

EP - 1131

JO - Journal of Medicinal Chemistry

JF - Journal of Medicinal Chemistry

SN - 0022-2623

IS - 3

ER -

Synthesis and structure-activity relationship studies of N-terminal analogues of the antimicrobial peptide tridecaptin A(1)

Abstract

Keywords

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Stephen Cochrane

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