Side-chain-to-tail thiolactone peptide inhibitors of the staphylococcal quorum-sensing system

R. John Scott; Lu Yun Lian; S. Hanna Muharram; Alan Cockayne; Stewart J. Wood; Barrie W. Bycroft; Paul Williams; Weng C. Chan

doi:10.1016/S0960-894X(03)00497-9

Side-chain-to-tail thiolactone peptide inhibitors of the staphylococcal quorum-sensing system

R. John Scott, Lu Yun Lian, S. Hanna Muharram, Alan Cockayne, Stewart J. Wood, Barrie W. Bycroft, Paul Williams, Weng C. Chan

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

Abstract

The expression of many staphylococcal virulence factors are regulated by the agr locus via a two-component signal transduction system (TCSTS), which is activated in response to a secreted autoinducer peptide (AIP). By exploiting the unique chemical architecture of the naturally occurring AIP-1, several potent inhibitors of staphylococcal TCSTS were designed and synthesized using either a linear or branched solid-phase approach. These inhibitors are competitive binders and contain the crucial 16-membered side-chain-to-tail thiolactone peptide pharmacophore. © 2003 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	2449-2453
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	13
Issue number	15
DOIs	https://doi.org/10.1016/S0960-894X(03)00497-9
Publication status	Published - 4 Aug 2003

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title = "Side-chain-to-tail thiolactone peptide inhibitors of the staphylococcal quorum-sensing system",

abstract = "The expression of many staphylococcal virulence factors are regulated by the agr locus via a two-component signal transduction system (TCSTS), which is activated in response to a secreted autoinducer peptide (AIP). By exploiting the unique chemical architecture of the naturally occurring AIP-1, several potent inhibitors of staphylococcal TCSTS were designed and synthesized using either a linear or branched solid-phase approach. These inhibitors are competitive binders and contain the crucial 16-membered side-chain-to-tail thiolactone peptide pharmacophore. {\textcopyright} 2003 Elsevier Ltd. All rights reserved.",

author = "Scott, {R. John} and Lian, {Lu Yun} and Muharram, {S. Hanna} and Alan Cockayne and Wood, {Stewart J.} and Bycroft, {Barrie W.} and Paul Williams and Chan, {Weng C.}",

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T1 - Side-chain-to-tail thiolactone peptide inhibitors of the staphylococcal quorum-sensing system

AU - Scott, R. John

AU - Lian, Lu Yun

AU - Muharram, S. Hanna

AU - Cockayne, Alan

AU - Wood, Stewart J.

AU - Bycroft, Barrie W.

AU - Williams, Paul

AU - Chan, Weng C.

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Y1 - 2003/8/4

N2 - The expression of many staphylococcal virulence factors are regulated by the agr locus via a two-component signal transduction system (TCSTS), which is activated in response to a secreted autoinducer peptide (AIP). By exploiting the unique chemical architecture of the naturally occurring AIP-1, several potent inhibitors of staphylococcal TCSTS were designed and synthesized using either a linear or branched solid-phase approach. These inhibitors are competitive binders and contain the crucial 16-membered side-chain-to-tail thiolactone peptide pharmacophore. © 2003 Elsevier Ltd. All rights reserved.

AB - The expression of many staphylococcal virulence factors are regulated by the agr locus via a two-component signal transduction system (TCSTS), which is activated in response to a secreted autoinducer peptide (AIP). By exploiting the unique chemical architecture of the naturally occurring AIP-1, several potent inhibitors of staphylococcal TCSTS were designed and synthesized using either a linear or branched solid-phase approach. These inhibitors are competitive binders and contain the crucial 16-membered side-chain-to-tail thiolactone peptide pharmacophore. © 2003 Elsevier Ltd. All rights reserved.

U2 - 10.1016/S0960-894X(03)00497-9

DO - 10.1016/S0960-894X(03)00497-9

M3 - Article

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SN - 1464-3405

VL - 13

SP - 2449

EP - 2453

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 15

ER -

Side-chain-to-tail thiolactone peptide inhibitors of the staphylococcal quorum-sensing system

Abstract

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