| Literature DB >> 27125019 |
M N Berlov, E S Umnyakova, T S Leonova, B L Milman, A D Krasnodembskaya, T V Ovchinnikova, V N Kokryakov.
Abstract
The interaction between arenicin-1, that is an antimicrobial peptide from polychaeta Arenicola marina, and human complement system protein C1q was studied using enzyme-linked receptor sorbent assay and ELISA. We revealed that arenicin-1 and C1q form complex that is stable in high ionic strength condition 0.5 M NaCl. The ability of C1q to interact with arenicin-1 is comparable with the binding activity of C1q towards another antimicrobial peptide, porcine cathelicidin protegrin-1, which has a similar spatial arrangement with arenicin-1. Namely, both arenicin-1 and protegrin-1 form cystine-stabilized antiparallel β-hairpin structure.Entities:
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Year: 2015 PMID: 27125019 DOI: 10.1134/s1068162015060035
Source DB: PubMed Journal: Bioorg Khim ISSN: 0132-3423