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Cobra Cytotoxins: Structural Organization and Antibacterial Activity
Cardiotoxins (cytotoxins, CT) are β-structured proteins isolated from the venom of cobra. They consist of 59–61 amino acid residues, whose antiparallel chains form three ‘fingers’. In contrast to neurotoxins with an overall similar fold, CTs are amphiphilic. The amphiphilicity is caused by positivel...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
A.I. Gordeyev
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4207557/ https://www.ncbi.nlm.nih.gov/pubmed/25349711 |
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author | Dubovskii, P. V. Utkin, Y. N. |
author_facet | Dubovskii, P. V. Utkin, Y. N. |
author_sort | Dubovskii, P. V. |
collection | PubMed |
description | Cardiotoxins (cytotoxins, CT) are β-structured proteins isolated from the venom of cobra. They consist of 59–61 amino acid residues, whose antiparallel chains form three ‘fingers’. In contrast to neurotoxins with an overall similar fold, CTs are amphiphilic. The amphiphilicity is caused by positively charged lysine and arginine residues flanking the tips of the loops that consist primarily of hydrophobic amino acids. A similar distribution of amino acid residues is typical for linear (without disulfide bonds) cationic cytolytic peptides from the venoms of other snakes and insects. Many of them are now considered to be lead compounds in combatting bacterial infections and cancer. In the present review, we summarize the data on the antibacterial activity of CTs and compare it to the activity of linear peptides. |
format | Online Article Text |
id | pubmed-4207557 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | A.I. Gordeyev |
record_format | MEDLINE/PubMed |
spelling | pubmed-42075572014-10-27 Cobra Cytotoxins: Structural Organization and Antibacterial Activity Dubovskii, P. V. Utkin, Y. N. Acta Naturae Research Article Cardiotoxins (cytotoxins, CT) are β-structured proteins isolated from the venom of cobra. They consist of 59–61 amino acid residues, whose antiparallel chains form three ‘fingers’. In contrast to neurotoxins with an overall similar fold, CTs are amphiphilic. The amphiphilicity is caused by positively charged lysine and arginine residues flanking the tips of the loops that consist primarily of hydrophobic amino acids. A similar distribution of amino acid residues is typical for linear (without disulfide bonds) cationic cytolytic peptides from the venoms of other snakes and insects. Many of them are now considered to be lead compounds in combatting bacterial infections and cancer. In the present review, we summarize the data on the antibacterial activity of CTs and compare it to the activity of linear peptides. A.I. Gordeyev 2014 /pmc/articles/PMC4207557/ /pubmed/25349711 Text en Copyright ® 2014 Park-media Ltd. http://creativecommons.org/licenses/by/2.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Dubovskii, P. V. Utkin, Y. N. Cobra Cytotoxins: Structural Organization and Antibacterial Activity |
title | Cobra Cytotoxins: Structural Organization and Antibacterial Activity |
title_full | Cobra Cytotoxins: Structural Organization and Antibacterial Activity |
title_fullStr | Cobra Cytotoxins: Structural Organization and Antibacterial Activity |
title_full_unstemmed | Cobra Cytotoxins: Structural Organization and Antibacterial Activity |
title_short | Cobra Cytotoxins: Structural Organization and Antibacterial Activity |
title_sort | cobra cytotoxins: structural organization and antibacterial activity |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4207557/ https://www.ncbi.nlm.nih.gov/pubmed/25349711 |
work_keys_str_mv | AT dubovskiipv cobracytotoxinsstructuralorganizationandantibacterialactivity AT utkinyn cobracytotoxinsstructuralorganizationandantibacterialactivity |