Název:
Design of stable antimicrobial peptides through hydrocarbon stapling
Autoři:
Chapuis, Hubert Jean ; Slaninová, Jiřina ; Monincová, Lenka ; Bednárová, Lucie ; Čeřovský, Václav Typ dokumentu: Příspěvky z konference Konference/Akce: Biologically Active Peptides /12./, Praha (CZ), 2011-04-27 / 2011-04-29
Rok:
2011
Jazyk:
eng
Abstrakt: 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.
Klíčová slova:
amphipathic alpha-helices; antimicrobial peptides; peptide stapling; peptide synthesis; ring closing metathesis (RCM) Číslo projektu: CEZ:AV0Z40550506 (CEP), GA203/08/0536 (CEP) Poskytovatel projektu: GA ČR Zdrojový dokument: Biologically Active Peptides. 12th Conference, ISBN 978-80-86241-44-9
Instituce: Ústav organické chemie a biochemie AV ČR
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Informace o dostupnosti dokumentu:
Dokument je dostupný v příslušném ústavu Akademie věd ČR. Původní záznam: http://hdl.handle.net/11104/0203990