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.
Original language | English |
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Pages (from-to) | 664-668 |
Number of pages | 5 |
Journal | BIOORGANICHESKAYA KHIMIYA |
Volume | 41 |
Issue number | 6 |
DOIs | |
Publication status | Published - 01 Nov 2015 |
ASJC Scopus subject areas
- General Medicine