Mostrar el registro sencillo del ítem

dc.creatorLomonte, Bruno
dc.creatorAngulo Ugalde, Yamileth
dc.creatorMoreno Robles, Edgardo
dc.date.accessioned2018-03-13T15:24:07Z
dc.date.available2018-03-13T15:24:07Z
dc.date.issued2010
dc.identifier.issn1381-6128
dc.identifier.issn1873-4286
dc.identifier.urihttp://hdl.handle.net/10669/74297
dc.description.abstractLys49-phospholipase A2 homologues constitute a large family of toxins present in the venoms of viperid snake species, which despite lacking catalytic activity, cause significant skeletal muscle necrosis. The main structural determinants of this toxic effect have been experimentally mapped to a region near their C-terminus (115-129), which combines cationic and hydrophobic/aromatic amino acid residues. Short (13-mer) synthetic peptides representing this C-terminal region can mimick several of the effects of Lys49 PLA2 homologues. In addition to their ability to damage muscle cells, these peptides display antibacterial, antiendotoxic, antifungal, antiparasite, and antitumor activities, as well as VEGF-receptor 2 (KDR)-binding and heparin-binding properties. Modifications of their sequences have shown possibilities to enhance their effects upon prokaryotic cells, while decreasing toxicity for eukaryotic cells. This review presents an updated summary on the biomimetic actions exerted by such peptides, and highlights their potential value as molecular tools or as drug leads in diverse biomedical areas.es_ES
dc.description.sponsorshipUniversidad de Costa Rica//UCR/Costa Ricaes_ES
dc.description.sponsorshipInternational Foundation for Science//IFS/Sueciaes_ES
dc.description.sponsorshipConsejo Nacional para Investigaciones Científicas y Tecnológicas//CONICIT/Costa Ricaes_ES
dc.description.sponsorshipNetwork for Research and Training in Tropical Diseases in Central America//NeTropica/es_ES
dc.description.sponsorshipFundación Costa Rica - Estados Unidos para la Cooperación//CRUSA/Estados Unidoses_ES
dc.description.sponsorshipEmbajada de Japónv en Costa Rica///Japónes_ES
dc.description.sponsorshipLindbergh Foundation///Estados Unidoses_ES
dc.description.sponsorshipAmerican Society for Microbiology///Estados Unidoses_ES
dc.description.sponsorshipFlorida Ice & Farm///Costa Ricaes_ES
dc.description.sponsorshipConsejo Superior de Investigaciones Científicas//CSIC/Españaes_ES
dc.description.sponsorshipConsejo Nacional de Rectores//CONARE/Costa Ricaes_ES
dc.description.sponsorshipInternational Centre for Genetic Engineering and Biotechnology//ICGEB-CRP/Italiaes_ES
dc.language.isoen_USes_ES
dc.rightsCC0 1.0 Universal*
dc.rights.urihttp://creativecommons.org/publicdomain/zero/1.0/*
dc.sourceCurrent Pharmaceutical Design, vol. 16, 3224-3230es_ES
dc.subjectPhospholipase A2es_ES
dc.subjectMyotoxines_ES
dc.subjectSynthetic peptideses_ES
dc.subjectSnake venomes_ES
dc.subjectAntitumores_ES
dc.titleSynthetic peptides derived from the C-terminal region of Lys49 phospholipase A2 homologues from Viperidae snake venoms: biomimetic activities and potential applicationses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.2174/138161210793292456
dc.description.procedenceUCR::Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.description.procedenceUCR::Docencia::Salud::Facultad de Medicina::Escuela de Medicinaes_ES
dc.identifier.pmid20687875


Ficheros en el ítem

Thumbnail
Thumbnail

Este ítem aparece en la(s) siguiente(s) colección(ones)

Mostrar el registro sencillo del ítem

CC0 1.0 Universal
Excepto si se señala otra cosa, la licencia del ítem se describe como CC0 1.0 Universal