Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator
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...
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| Format: | Article |
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MDPI AG
2020-12-01
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| Series: | Marine Drugs |
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| Online Access: | https://www.mdpi.com/1660-3397/18/12/631 |
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| author | Ilia A. Krenev 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 Mikhail N. Berlov |
| author_facet | Ilia A. Krenev 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 Mikhail N. Berlov |
| author_sort | Ilia A. Krenev |
| collection | DOAJ |
| description | 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 <i>Arenicola marina</i>, 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. |
| first_indexed | 2024-03-10T14:10:31Z |
| format | Article |
| id | doaj.art-2ea4dad3a6164fce8e7f5b6022fa0dad |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-03-10T14:10:31Z |
| publishDate | 2020-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-2ea4dad3a6164fce8e7f5b6022fa0dad2023-11-21T00:14:06ZengMDPI AGMarine Drugs1660-33972020-12-01181263110.3390/md18120631Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System ModulatorIlia A. Krenev0Ekaterina S. Umnyakova1Igor E. Eliseev2Yaroslav A. Dubrovskii3Nikolay P. Gorbunov4Vladislav A. Pozolotin5Alexei S. Komlev6Pavel V. Panteleev7Sergey V. Balandin8Tatiana V. Ovchinnikova9Olga V. Shamova10Mikhail N. Berlov11Department of General Pathology and Pathological Physiology, Institute of Experimental Medicine, Acad. Pavlov Str. 12, 197376 Saint Petersburg, RussiaDepartment of General Pathology and Pathological Physiology, Institute of Experimental Medicine, Acad. Pavlov Str. 12, 197376 Saint Petersburg, RussiaNanobiotechnology Laboratory, Alferov University, Khlopin Str. 8/3, 194021 Saint Petersburg, RussiaFaculty of Chemistry, Saint Petersburg State University, Universitetskaya Emb, 7/9, 199034 Saint Petersburg, RussiaDepartment of General Pathology and Pathological Physiology, Institute of Experimental Medicine, Acad. Pavlov Str. 12, 197376 Saint Petersburg, RussiaDepartment of General Pathology and Pathological Physiology, Institute of Experimental Medicine, Acad. Pavlov Str. 12, 197376 Saint Petersburg, RussiaDepartment of General Pathology and Pathological Physiology, Institute of Experimental Medicine, Acad. Pavlov Str. 12, 197376 Saint Petersburg, RussiaM.M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str., 16/10, 117997 Moscow, RussiaM.M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str., 16/10, 117997 Moscow, RussiaM.M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str., 16/10, 117997 Moscow, RussiaDepartment of General Pathology and Pathological Physiology, Institute of Experimental Medicine, Acad. Pavlov Str. 12, 197376 Saint Petersburg, RussiaDepartment of General Pathology and Pathological Physiology, Institute of Experimental Medicine, Acad. Pavlov Str. 12, 197376 Saint Petersburg, RussiaAntimicrobial 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 <i>Arenicola marina</i>, 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.https://www.mdpi.com/1660-3397/18/12/631antimicrobial peptidearenicincomplement systemcomplement regulation |
| spellingShingle | Ilia A. Krenev 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 Mikhail N. Berlov Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator Marine Drugs antimicrobial peptide arenicin complement system complement regulation |
| title | Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator |
| title_full | Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator |
| title_fullStr | Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator |
| title_full_unstemmed | Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator |
| title_short | Antimicrobial Peptide Arenicin-1 Derivative Ar-1-(C/A) as Complement System Modulator |
| title_sort | antimicrobial peptide arenicin 1 derivative ar 1 c a as complement system modulator |
| topic | antimicrobial peptide arenicin complement system complement regulation |
| url | https://www.mdpi.com/1660-3397/18/12/631 |
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