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

doi:10.1134/S1068162015060035

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

School of Medicine, Dentistry and Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	597-601
Journal	Russian Journal of Bioorganic Chemistry
Volume	41
Issue number	6
DOIs	https://doi.org/10.1134/S1068162015060035
Publication status	Published - 20 Nov 2015

Keywords

antimicrobial peptides
arenicins
C1q
complement
protein-protein interactions
β structure

ASJC Scopus subject areas

Biochemistry
Organic Chemistry

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title = "Interaction of arenicin-1 with C1q protein",

abstract = "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).",

keywords = "antimicrobial peptides, arenicins, C1q, complement, protein-protein interactions, β structure",

author = "Berlov, {M. N.} and Umnyakova, {E. S.} and Leonova, {T. S.} and Milman, {B. L.} and Krasnodembskaya, {A. D.} and Ovchinnikova, {T. V.} and Kokryakov, {V. N.}",

year = "2015",

month = nov,

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doi = "10.1134/S1068162015060035",

language = "English",

volume = "41",

pages = "597--601",

journal = "Russian Journal of Bioorganic Chemistry",

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publisher = "Maik Nauka-Interperiodica Publishing",

number = "6",

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TY - JOUR

T1 - Interaction of arenicin-1 with C1q protein

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 - 2015/11/20

Y1 - 2015/11/20

N2 - 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).

AB - 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).

KW - antimicrobial peptides

KW - arenicins

KW - C1q

KW - complement

KW - protein-protein interactions

KW - β structure

U2 - 10.1134/S1068162015060035

DO - 10.1134/S1068162015060035

M3 - Article

AN - SCOPUS:84947918238

SN - 1068-1620

VL - 41

SP - 597

EP - 601

JO - Russian Journal of Bioorganic Chemistry

JF - Russian Journal of Bioorganic Chemistry

IS - 6

ER -

Interaction of arenicin-1 with C1q protein

Abstract

Keywords

ASJC Scopus subject areas

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