title: [Interaction of Arenicin-1 with C1q Protein].
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.
authors.forename: M N
authors.initials: MN
authors.lastname: Berlov
authors.forename: E S
authors.initials: ES
authors.lastname: Umnyakova
authors.forename: T S
authors.initials: TS
authors.lastname: Leonova
authors.forename: B L
authors.initials: BL
authors.lastname: Milman
authors.forename: A D
authors.initials: AD
authors.lastname: Krasnodembskaya
authors.forename: T V
authors.initials: TV
authors.lastname: Ovchinnikova
authors.forename: V N
authors.initials: VN
authors.lastname: Kokryakov
mesh_terms: D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D015922:Complement C1q / Q000737:chemistry*; D015801:Helminth Proteins / Q000737:chemistry*; D006801:Humans; D020836:Protein Structure, Quaternary; D011817:Rabbits; D013552:Swine
chemical_list: D023181:Antimicrobial Cationic Peptides; D015801:Helminth Proteins; C496888:arenicin-1, Arenicola marina; D015922:Complement C1q