Crotamine and crotalicidin, membrane active peptides from Crotalus durissus terrificus rattlesnake venom, and their structurally-minimized fragments for applications in medicine and biotechnology
•Crotamine and crotalicidin, bioactive and multifunctional venom peptides.•Crotamine and crotalicidin are related to AMPs from mammals and reptiles.•NrTPs, crotamine-derived, display cell-penetrating and cargo-delivery capabilities.•Crotalicidin (vipericidin) is a cathelicidin expressed in the rattl...
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Published in: | Peptides (New York, N.Y. : 1980) Vol. 126; p. 170234 |
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Main Authors: | , |
Format: | Journal Article |
Language: | English |
Published: |
United States
Elsevier Inc
01-04-2020
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Subjects: | |
Online Access: | Get full text |
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Summary: | •Crotamine and crotalicidin, bioactive and multifunctional venom peptides.•Crotamine and crotalicidin are related to AMPs from mammals and reptiles.•NrTPs, crotamine-derived, display cell-penetrating and cargo-delivery capabilities.•Crotalicidin (vipericidin) is a cathelicidin expressed in the rattlesnake venom gland.•Ctn[15–34], a crotalicidin peptide with anti-infective and antiproliferative effects.
A global public health crisis has emerged with the extensive dissemination of multidrug-resistant microorganisms. Antimicrobial peptides (AMPs) from plants and animals have represented promising tools to counteract those resistant pathogens due to their multiple pharmacological properties such as antimicrobial, anticancer, immunomodulatory and cell-penetrating activities. In this review, we will focus on crotamine and crotalicidin, which are two interesting examples of membrane active peptides derived from the South America rattlesnake Crotalus durrisus terrificus venom. Their full-sequences and structurally-minimized fragments have potential applications, as anti-infective and anti-proliferative agents and diagnostics in medicine and in pharmaceutical biotechnology. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 0196-9781 1873-5169 |
DOI: | 10.1016/j.peptides.2019.170234 |