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 ß-hairpin stabilized by disulfide bridges).
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Abbreviations
- AMPs:
-
antimicrobial peptides
- PBS0:
-
0.01 M phosphate buffered saline
- pH 7.4:
-
supplemented with 0.15 M NaCl
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Original Russian Text © M.N. Berlov, E.S. Umnyakova, T.S. Leonova, B.L. Milman, A.D. Krasnodembskaya, T.V. Ovchinnikova, V.N. Kokryakov, 2015, published in Bioorganicheskaya Khimiya, 2015, Vol. 41, No. 6, pp. 664–668.
The article has been adapted from the report presented at the VIIth All-Russian symposium “Proteins and Peptides”, Novosibirsk, 12–17 July, 2015.
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Berlov, M.N., Umnyakova, E.S., Leonova, T.S. et al. Interaction of arenicin-1 with C1q protein. Russ J Bioorg Chem 41, 597–601 (2015). https://doi.org/10.1134/S1068162015060035
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DOI: https://doi.org/10.1134/S1068162015060035