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

doi:10.7868/s0132342315060032

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 journal › Article › peer-review

2 Citations (Scopus)

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
Pages (from-to)	664-668
Number of pages	5
Journal	BIOORGANICHESKAYA KHIMIYA
Volume	41
Issue number	6
DOIs	https://doi.org/10.7868/s0132342315060032
Publication status	Published - 01 Nov 2015

ASJC Scopus subject areas

General Medicine

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title = "Interaction of arenicin-1 with C1q protein. Article in Russian.",

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.",

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doi = "10.7868/s0132342315060032",

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AU - Berlov, M. N.

AU - Umnyakova, E. S.

AU - Leonova, T. S.

AU - Milman, B. L.

AU - Krasnodembskaya, A. D.

AU - Ovchinnikova, T. V.

AU - Kokryakov, V. N.

PY - 2015/11/1

Y1 - 2015/11/1

N2 - 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.

AB - 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.

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JF - BIOORGANICHESKAYA KHIMIYA

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ER -

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

Abstract

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