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Biochim Biophys Acta Biomembr ; 1864(10): 183996, 2022 10 01.
Artigo em Inglês | MEDLINE | ID: mdl-35753394

RESUMO

The treatment of invasive drug-resistant and potentially life-threatening fungal infections is limited to few therapeutic options that are usually associated with severe side effects. The development of new effective antimycotics with a more tolerable side effect profile is therefore of utmost clinical importance. Here, we used a combination of complementary in vitro assays and structural analytical methods to analyze the interaction of the de novo antimicrobial peptide VG16KRKP with the sterol moieties of biological cell membranes. We demonstrate that VG16KRKP disturbs the structural integrity of fungal membranes both invitro and in model membrane system containing ergosterol along with phosphatidylethanolamine lipid and exhibits broad-spectrum antifungal activity. As revealed by systematic structure-function analysis of mutated VG16KRKP analogs, a specific pattern of basic and hydrophobic amino acid side chains in the primary peptide sequence determines the selectivity of VG16KRKP for fungal specific membranes.


Assuntos
Antifúngicos , Ergosterol , Antifúngicos/química , Antifúngicos/farmacologia , Membrana Celular/metabolismo , Ergosterol/química , Peptídeos/química , Peptídeos/farmacologia , Esteróis/metabolismo
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