Interaction of arenicin-1 with C1q protein

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

4 Citations (Scopus)


The interaction of arenicin-1, an antimicrobial peptide from the lugworm Arenicola marina with the protein C1q of the human complement system has been analyzed using enzyme-linked receptor sorbent assay and ELISA. Arenicin-1 and C1q were shown to form a stable complex that persisted at elevated ionic strength (0.5 M NaCl). The ability of arenicin-1 to interact with C1q is comparable to that of the porcine cathelicidin protegrin-1, an antimicrobial peptide that has a spatial structure similar to that of arenicin (an antiparallel β-hairpin stabilized by disulfide bridges).

Original languageEnglish
Pages (from-to)597-601
JournalRussian Journal of Bioorganic Chemistry
Issue number6
Publication statusPublished - 20 Nov 2015


  • antimicrobial peptides
  • arenicins
  • C1q
  • complement
  • protein-protein interactions
  • β structure

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry


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