Počet záznamů: 1
Structural Basis for Antimicrobial Activity of Lasiocepsin
- 1.0427641 - ÚOCHB 2015 RIV DE eng J - Článek v odborném periodiku
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
Grant CEP: GA ČR GA203/08/0536; GA MŠMT(CZ) LK11205
Institucionální podpora: RVO:61388963
Klíčová slova: antimicrobial peptides * Lasioglossum laticeps * membranes * NMR spectroscopy * ShK family
Kód oboru RIV: CE - Biochemie
Impakt faktor: 3.088, rok: 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.
Trvalý link: http://hdl.handle.net/11104/0233164
Počet záznamů: 1