alexa Scorpine-Like Peptides
ISSN: 2168-9431

Single Cell Biology
Open Access

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Scorpine-Like Peptides

Karen Luna-Ramírez1, Juana Maria Jiménez-Vargas2 and Lourival D Possani2*

1Department of Bioresources, Fraunhofer Institute for Molecular Biology and Applied Ecology, Winchester Str. 2, 35394 Giessen, Germany

2Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca 62210, México

Corresponding Author:
Lourival D Possani
Departamento de Medicina Molecular y Bioprocesos
Instituto de Biotecnología, Universidad Nacional Autónoma
de México, Avenida Universidad, 2001, Colonia Chamilpa Apartado
Postal 510-3, Cuernavaca 62210, México
Tel: +52-77-73121709
Fax: +52-77-73172388
E-mail: [email protected]

Received date: April 05, 2016; Accepted date: May 07, 2016; Published date: May 09, 2016

Citation: Luna-Ramírez K, Jiménez-Vargas JM, Possani LD (2016) Scorpine-Like Peptides. Single Cell Biol 5:138. doi:10.4172/2168-9431.1000138

Copyright: © 2016 Luna-Ramírez K, et al. 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 author and source are credited.



Scorpine-like peptides are intriguing and unique compounds of scorpion venom. They possess two well-defined regions that confers them bi-functionality. The N-terminal region is similar to scorpion antimicrobial peptides lacking disulfide bridges, whereas the C-terminal region contains six cysteines forming three disulfide bridges that tightly bind the peptide. Scorpine-like peptides have shown activity against bacteria (i.e. B. subtilis, K. pneumoniae, P. aeruginosa), fungi and also as potassium channel blockers. Additionally, they have been successful in controlling malaria and some types of viruses.


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