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Structure Elucidation and Functional Studies of a Novel β-hairpin Antimicrobial Peptide from the Marine Polychaeta Capitella teleta

Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator

Department of General Pathology and Pathological Physiology, Institute of Experimental Medicine, Acad. Pavlov Str. 12, 197376 Saint Petersburg, Russia
Faculty of Chemistry, Saint Petersburg State University, Universitetskaya Emb, 7/9, 199034 Saint Petersburg, Russia
Nanobiotechnology Laboratory, Alferov University, Khlopin Str. 8/3, 194021 Saint Petersburg, Russia
Almazov National Medical Research Centre, Akkuratov Str, 2, 197341 Saint Petersburg, Russia
M.M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str., 16/10, 117997 Moscow, Russia
Department of Biotechnology, I.M. Sechenov First Moscow State Medical University, Trubetskaya Str., 8-2, 119991 Moscow, Russia
Author to whom correspondence should be addressed.
Mar. Drugs 2020, 18(12), 631;
Received: 3 November 2020 / Revised: 27 November 2020 / Accepted: 8 December 2020 / Published: 10 December 2020
Antimicrobial peptides (AMPs) are not only cytotoxic towards host pathogens or cancer cells but also are able to act as immunomodulators. It was shown that some human and non-human AMPs can interact with complement proteins and thereby modulate complement activity. Thus, AMPs could be considered as the base for complement-targeted therapeutics development. Arenicins from the sea polychaete Arenicola marina, the classical example of peptides with a β-hairpin structure stabilized by a disulfide bond, were shown earlier to be among the most prospective regulators. Here, we investigate the link between arenicins’ structure and their antimicrobial, hemolytic and complement-modulating activities using the derivative Ar-1-(C/A) without a disulfide bond. Despite the absence of this bond, the peptide retains all important functional activities and also appears less hemolytic in comparison with the natural forms. These findings could help to investigate new complement drugs for regulation using arenicin derivatives. View Full-Text
Keywords: antimicrobial peptide; arenicin; complement system; complement regulation antimicrobial peptide; arenicin; complement system; complement regulation
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MDPI and ACS Style

Krenev, I.A.; Umnyakova, E.S.; Eliseev, I.E.; Dubrovskii, Y.A.; Gorbunov, N.P.; Pozolotin, V.A.; Komlev, A.S.; Panteleev, P.V.; Balandin, S.V.; Ovchinnikova, T.V.; Shamova, O.V.; Berlov, M.N. Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator. Mar. Drugs 2020, 18, 631.

AMA Style

Krenev IA, Umnyakova ES, Eliseev IE, Dubrovskii YA, Gorbunov NP, Pozolotin VA, Komlev AS, Panteleev PV, Balandin SV, Ovchinnikova TV, Shamova OV, Berlov MN. Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator. Marine Drugs. 2020; 18(12):631.

Chicago/Turabian Style

Krenev, Ilia A., Ekaterina S. Umnyakova, Igor E. Eliseev, Yaroslav A. Dubrovskii, Nikolay P. Gorbunov, Vladislav A. Pozolotin, Alexei S. Komlev, Pavel V. Panteleev, Sergey V. Balandin, Tatiana V. Ovchinnikova, Olga V. Shamova, and Mikhail N. Berlov 2020. "Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator" Marine Drugs 18, no. 12: 631.

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