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

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Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator. / Krenev, Ilia A.; Umnyakova, Ekaterina S.; Eliseev, Igor E.; Dubrovskii, Yaroslav A.; Gorbunov, Nikolay P.; Pozolotin, Vladislav A.; Komlev, Alexei S.; Panteleev, Pavel V.; Balandin, Sergey V.; Ovchinnikova, Tatiana V.; Shamova, Olga V.; Berlov, Mikhail N.

In: Marine Drugs, Vol. 18, No. 12, 10.12.2020.

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

Author

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

BibTeX

@article{4bbab5f7ad6346f1b0f40bd3d95d84c7,

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

abstract = "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.",

keywords = "antimicrobial peptide, arenicin, complement regulation, complement system",

author = "Krenev, {Ilia A.} and Umnyakova, {Ekaterina S.} and Eliseev, {Igor E.} and Dubrovskii, {Yaroslav A.} and Gorbunov, {Nikolay P.} and Pozolotin, {Vladislav A.} and Komlev, {Alexei S.} and Panteleev, {Pavel V.} and Balandin, {Sergey V.} and Ovchinnikova, {Tatiana V.} and Shamova, {Olga V.} and Berlov, {Mikhail N.}",

year = "2020",

month = dec,

day = "10",

doi = "10.3390/md18120631",

language = "English",

volume = "18",

journal = "Marine Drugs",

issn = "1660-3397",

publisher = "MDPI AG",

number = "12",

}

RIS

TY - JOUR

T1 - Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator

AU - Krenev, Ilia A.

AU - Umnyakova, Ekaterina S.

AU - Eliseev, Igor E.

AU - Dubrovskii, Yaroslav A.

AU - Gorbunov, Nikolay P.

AU - Pozolotin, Vladislav A.

AU - Komlev, Alexei S.

AU - Panteleev, Pavel V.

AU - Balandin, Sergey V.

AU - Ovchinnikova, Tatiana V.

AU - Shamova, Olga V.

AU - Berlov, Mikhail N.

PY - 2020/12/10

Y1 - 2020/12/10

N2 - 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.

AB - 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.

KW - antimicrobial peptide

KW - arenicin

KW - complement regulation

KW - complement system

UR - http://www.scopus.com/inward/record.url?scp=85098533917&partnerID=8YFLogxK

U2 - 10.3390/md18120631

DO - 10.3390/md18120631

M3 - Article

C2 - 33321960

AN - SCOPUS:85098533917

VL - 18

JO - Marine Drugs

JF - Marine Drugs

SN - 1660-3397

IS - 12

ER -

ID: 85161155