Advances in Biomedical Spectroscopy

0425093 - ÚOCHB 2014 NL eng M - Monography Chapter
Pazderková, Markéta - Kočišová, E. - Pazderka, T. - Maloň, Petr - Kopecký, V. Jr. - Monincová, Lenka - Čeřovský, Václav - Bednárová, Lucie
Antimicrobial peptide from the eusocial bee Halictus sexcinctus interacting with model membranes.
Advances in Biomedical Spectroscopy. Amsterdam: IOS Press, 2013 - (Marques, M.; Batista de Carvalho, L.; Haris, P.), s. 79-83. Spectroscopy of Biological Molecules, 7. ISBN 978-1-61499-183-0
Institutional research plan: CEZ:AV0Z40550506
Keywords : antibacterial peptides * circular dichroism * fluorescence * halictine * infrared spectroscopy * liposome * micelle * phospholipid
Subject RIV: CC - Organic Chemistry

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's ability to adopt an amphipathic α-helical structure upon interaction with model lipid based bacterial membranes (phosphatidylcholine/phosphatidylglycerol based large unilamellar vesicles, sodium dodecylsulfate micelles) and helix inducing components (trifluoroethanol). It was found that Hal-1 responds sensitively to composition of the membrane model and to peptide/lipid ratio. Amphipathic nature of the helical Hal-1 seems to favour flat charged surfaces of the model lipid particles over the non-directional interaction with trifluoroethanol. Increasing fraction of polyproline II type conformation was detected at low peptide/lipid ratios.
Permanent Link: http://hdl.handle.net/11104/0231031