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Melectin: A novel antimicrobial peptide from the venom of the cleptoparasitic bee Melecta albifrons
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SYSNO ASEP 0315415 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Melectin: A novel antimicrobial peptide from the venom of the cleptoparasitic bee Melecta albifrons Title Melectin: Nový antimikrobiální peptid z jedu kleptoparasitické včely Melecta albifrons Author(s) Čeřovský, Václav (UOCHB-X) RID, ORCID
Hovorka, Oldřich (UOCHB-X)
Cvačka, Josef (UOCHB-X) RID, ORCID
Voburka, Zdeněk (UOCHB-X)
Bednárová, Lucie (UOCHB-X) RID, ORCID
Borovičková, Lenka (UOCHB-X)
Slaninová, Jiřina (UOCHB-X)
Fučík, Vladimír (UOCHB-X) RIDSource Title Chembiochem. - : Wiley - ISSN 1439-4227
Roč. 9, č. 17 (2008), s. 2815-2821Number of pages 7 s. Language eng - English Country DE - Germany Keywords amphipathicity ; antimicrobial activity ; helical structures ; peptides ; solitary bee venom 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 000261483200012 DOI 10.1002/cbic.200800476 Annotation A novel antimicrobial peptide H-Gly-Phe-Leu-Ser-Ile-Leu-Lys-Lys-Val-Leu-Pro-Lys-Val-Met-Ala-His-Met-Lys-NH2 designated melectin was firstly identified in solitary be venom. It possesses high antimicrobial activity against both Gram-positive and -negative bacteria and low hemolytic activity. As indicated by CD spectra, melectin can adopt an amphipathic alpha-helical secondary structure in an anisotropic environment such as the bacterial cell membrane. The presence of Pro residue in the central part of the molecule plays an important role in the biological activity of melectin. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Year of Publishing 2009
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