Original title: Design of stable antimicrobial peptides through hydrocarbon stapling
Authors: Chapuis, Hubert Jean ; Slaninová, Jiřina ; Monincová, Lenka ; Bednárová, Lucie ; Čeřovský, Václav
Document type: Papers
Conference/Event: Biologically Active Peptides /12./, Praha (CZ), 2011-04-27 / 2011-04-29
Year: 2011
Language: eng
Abstract: 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.
Keywords: amphipathic alpha-helices; antimicrobial peptides; peptide stapling; peptide synthesis; ring closing metathesis (RCM)
Project no.: CEZ:AV0Z40550506 (CEP), GA203/08/0536 (CEP)
Funding provider: GA ČR
Host item entry: Biologically Active Peptides. 12th Conference, ISBN 978-80-86241-44-9

Institution: Institute of Organic Chemistry and Biochemistry AS ČR (web)
Document availability information: Fulltext is available at the institute of the Academy of Sciences.
Original record: http://hdl.handle.net/11104/0203990

Permalink: http://www.nusl.cz/ntk/nusl-80987


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Research > Institutes ASCR > Institute of Organic Chemistry and Biochemistry
Conference materials > Papers