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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...

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Detalles Bibliográficos
Autores principales: Dubovskii, P. V., Utkin, Y. N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: A.I. Gordeyev 2014
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.
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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
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