Počet záznamů: 1  

Structural Basis for Antimicrobial Activity of Lasiocepsin

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    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  

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