Structural Basis for Antimicrobial Activity of Lasiocepsin. Issue 2 (12th December 2013)

• Record Type: Journal Article
• Authors: Monincová, Lenka; Buděšínský, Milos; Čujová, Sabina; Čeřovský, Václav; Veverka, Václav
• Is Part Of: Chembiochem. Volume 15:Issue 2(2014)
• Page Start: 301
• Page End: 308
• Publication Date: 2013-12-12
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201300509
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Lasiocepsin is a unique 27‐residue antimicrobial peptide, isolated from <italic>Lasioglossum laticeps</italic> (wild bee) venom, with substantial antibacterial and antifungal activity. It adopts a welldefined structure consisting of two α‐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.</p> </abstract>