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Effect of hydrocarbon stapling on the properties of alpha-helical antimicrobial peptides isolated from the venom of hymenoptera
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SYSNO ASEP 0384565 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Effect of hydrocarbon stapling on the properties of alpha-helical antimicrobial peptides isolated from the venom of hymenoptera Author(s) Chapuis, Hubert Jean (UOCHB-X)
Slaninová, Jiřina (UOCHB-X)
Bednárová, Lucie (UOCHB-X) RID, ORCID
Monincová, Lenka (UOCHB-X)
Buděšínský, Miloš (UOCHB-X) RID, ORCID
Čeřovský, Václav (UOCHB-X) RID, ORCIDNumber of authors 6 Source Title Amino Acids. - : Springer - ISSN 0939-4451
Roč. 43, č. 5 (2012), s. 2047-2058Number of pages 12 s. Language eng - English Country AT - Austria Keywords antimicrobial peptides ; stapled peptides ; amphipathic helix ; CD spectroscopy Subject RIV CC - Organic Chemistry R&D Projects GA203/08/0536 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z40550506 - UOCHB-X (2005-2011) UT WOS 000309863400022 DOI https://doi.org/10.1007/s00726-012-1283-1 Annotation Introducing all-hydrocarbon staples into short alpha-helical amphipathic antimicrobial peptides increases their hydrophobicity, hydrophobic moment, rigidity and generally alpha-helicity in water. Stapling generally makes the peptides more resistant to proteolytic degradation, particularly those that are doubly stapled. The introduction of olefinic amino acid residues and conformational restriction by stapling make the peptides significantly more hemolytic, and lead to a decrease of their antimicrobial potency against pathogenic bacteria. Unfortunately, the stapling of those peptides is not rendering compounds that would have better pharmacological qualities than the native unmodified potent peptides. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2013
Number of the records: 1