Structural Basis for Antimicrobial Activity of Lasiocepsin

0427641 - ÚOCHB 2015 RIV DE eng J - Journal Article
Monincová, Lenka - Buděšínský, Miloš - Čujová, Sabína - Čeřovský, Václav - Veverka, Václav
Structural Basis for Antimicrobial Activity of Lasiocepsin.
Chembiochem. Roč. 15, č. 2 (2014), s. 301-308. ISSN 1439-4227. E-ISSN 1439-7633
R&D Projects: GA ČR GA203/08/0536; GA MŠMT(CZ) LK11205
Institutional support: RVO:61388963
Keywords : antimicrobial peptides * Lasioglossum laticeps * membranes * NMR spectroscopy * ShK family
Subject RIV: CE - Biochemistry
Impact factor: 3.088, year: 2014

Lasiocepsin is a unique 27-residue antimicrobial peptide, isolated from Lasioglossum laticeps (wild bee) venom, with substantial antibacterial and antifungal activity. It adopts a welldefined structure consisting of two -helices linked by a structured loop. Its basic residues form two distinct positively charged regions on the surface whereas aliphatic side chains contribute to solvent-accessible hydrophobic areas, thus emphasising the amphipathic character of the molecule. Lasiocepsin structurally belongs to the ShK family and shows a strong preference for anionic phospholipids; this is further augmented by increasing concentrations of cardiolipin, such as those found at the poles of bacterial cells. The membrane-permeabilising activity of the peptide is not limited to outer membranes of Gram-negative bacteria. The peptide interacts with phospholipids initially through its N terminus, and its degree of penetration is strongly dependent on the presence of cardiolipin.
Permanent Link: http://hdl.handle.net/11104/0233164