0378834 - ÚOCHB 2013 RIV NL eng J - Journal Article
Pazderková, Markéta - Kočišová, E. - Pazderka, T. - Maloň, Petr - Kopecký ml., V. - Monincová, Lenka - Čeřovský, Václav - Bednárová, Lucie
Antimicrobial Peptide from the Eusocial Bee Halictus sexcinctus Interacting with Model Membranes.
Spectroscopy-an International Journal. Roč. 27, 5-6 (2012), s. 497-502. ISSN 0712-4813
R&D Projects: GA ČR GAP208/10/0376
Institutional research plan: CEZ:AV0Z40550506
Keywords : antibacterial peptides * halictine * micelle * liposome * phospholipid * circular dichroism * fluorescence * infrared spectroscopy
Subject RIV: CC - Organic Chemistry
Impact factor: 0.530, year: 2012

Halictine-1 (Hal-1)-a linear antibacterial dodecapeptide isolated from the venom of the eusocial bee Halictus sexcinctus-has been subjected to a detailed spectroscopic study including circular dichroism, fluorescence, and vibrational spectroscopy.We investigated Hal-1 ability to adopt an amphipathic alpha-helical structure upon interaction with model lipid-based bacterial membranes (phosphatidylcholine/phosphatidylglycerol-based large unilamellar vesicles and sodium dodecylsulfate micelles) and helix inducing components (trifluoroethanol). It was found that Hal-1 responds sensitively to the composition of the membrane model and to the peptide/lipid ratio. The amphipathic nature of the helical Hal-1 seems to favour flat charged surfaces of the model lipid particles over the nondirectional interaction with trifluoroethanol. Increasing fraction of polyproline II type conformation was detected at low peptide/lipid ratios.
Permanent Link: http://hdl.handle.net/11104/0210190