5m9u
From Proteopedia
Spatial structure of antimicrobial peptide arenicin-1 mutant V8R
Structural highlights
FunctionANN1_AREMA Has antimicrobial activity against the Gram-negative bacteria E.coli and P.mirabilis, the Gram-positive bacterium L.monocytogenes and the yeast C.albicans.[1] [2] Publication Abstract from PubMedThe beta-hairpin antimicrobial peptides arenicins from marine polychaeta Arenicola marina exhibit a broad spectrum of antimicrobial activity and high cytotoxicity. In this study the biological activities of arenicin-1 and its therapeutically valuable analog Ar-1[V8R] were investigated. The peptide Ar-1[V8R] displays significantly reduced cytotoxicity against mammalian cells relative to the wild-type arenicin-1. At the same time, both peptides exhibit similar antibacterial activities and kinetics of bacterial membrane permeabilization. Comparative NMR analysis of the peptides spatial structures in water and membrane-mimicking environment showed that Ar-1[V8R] in contrast to arenicin has significantly lower dimerization propensity. Thus, dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity. Dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity.,Panteleev PV, Myshkin MY, Shenkarev ZO, Ovchinnikova TV Biochem Biophys Res Commun. 2017 Jan 22;482(4):1320-1326. doi:, 10.1016/j.bbrc.2016.12.035. Epub 2016 Dec 8. PMID:27940358[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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