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Design of stable antimicrobial peptides through hydrocarbon stapling
- 1.0370086 - ÚOCHB 2012 CZ eng C - Conference Paper (international conference)
Chapuis, Hubert Jean - Slaninová, Jiřina - Monincová, Lenka - Bednárová, Lucie - Čeřovský, Václav
Design of stable antimicrobial peptides through hydrocarbon stapling.
Biologically Active Peptides. 12th Conference. Praha: Institute of Organic Chemistry and Biochemistry AS CR, v. v. i, 2011 - (Slaninová, J.), s. 19-21. Collection Symposium Series, 13. ISBN 978-80-86241-44-9.
[Biologically Active Peptides /12./. Praha (CZ), 27.04.2011-29.04.2011]
R&D Projects: GA ČR GA203/08/0536
Institutional research plan: CEZ:AV0Z40550506
Keywords : amphipathic alpha-helices * antimicrobial peptides * peptide synthesis * ring closing metathesis (RCM) * peptide stapling
Subject RIV: CC - Organic Chemistry
From the venom of wild bee Lasioglossum laticeps we have recently isolated novel antimicrobial peptides named lasioglossins. One of them, LL-III (VNWKKILGKIIKVVK-NH2), is an amphipathic α-helical peptide which shows strong antimicrobial properties and a low hemolytic activity. We anticipated that the incorporation of an all-hydrocarbon staple (bridge) into the LL-III sequence could increase its propensity to form an α-helix and lead to an improvement of its proteolytic stability as well as increase the antimicrobial activity. LL-III analogs featuring olefinic side chains in various positions were prepared by solid phase peptide synthesis. Ring closing olefin metatheses catalyzed by Grubbs-I catalyst were carried out on the solid support, either between i and i+4 positions or between i and i+7 positions.
Permanent Link: http://hdl.handle.net/11104/0203990
Number of the records: 1