Interaction of arenicin-1 with C1q protein. Article in Russian.

M. N. Berlov*, E. S. Umnyakova, T. S. Leonova, B. L. Milman, A. D. Krasnodembskaya, T. V. Ovchinnikova, V. N. Kokryakov

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


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 languageEnglish
Pages (from-to)664-668
Number of pages5
Issue number6
Publication statusPublished - 01 Nov 2015

ASJC Scopus subject areas

  • General Medicine


Dive into the research topics of 'Interaction of arenicin-1 with C1q protein. Article in Russian.'. Together they form a unique fingerprint.

Cite this