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(Reference retrieved automatically from SciELO through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Snake venom disintegrins update: insights about new findings

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Author(s):
Gabriela de Oliveira Almeida [1] ; Isadora Sousa de Oliveira ; Eliane Candiani Arantes [3] ; Suely Vilela Sampaio [4]
Total Authors: 4
Affiliation:
[1] University of São Paulo. School of Pharmaceutical Sciences of Ribeirão Preto. Department of Clinical Analysis, Toxicology and Food Science - Brasil
[3] University of São Paulo. School of Pharmaceutical Sciences of Ribeirão Preto. Department of BioMolecular Sciences - Brasil
[4] University of São Paulo. School of Pharmaceutical Sciences of Ribeirão Preto. Department of Clinical Analysis, Toxicology and Food Science - Brasil
Total Affiliations: 4
Document type: Journal article
Source: Journal of Venomous Animals and Toxins including Tropical Diseases; v. 29, 2023-09-18.
Abstract

ABSTRACT Snake venom disintegrins are low molecular weight, non-enzymatic proteins rich in cysteine, present in the venom of snakes from the families Viperidae, Crotalidae, Atractaspididae, Elapidae, and Colubridae. This family of proteins originated in venom through the proteolytic processing of metalloproteinases (SVMPs), which, in turn, evolved from a gene encoding an A Disintegrin And Metalloprotease (ADAM) molecule. Disintegrins have a recognition motif for integrins in their structure, allowing interaction with these transmembrane adhesion receptors and preventing their binding to proteins in the extracellular matrix and other cells. This interaction gives disintegrins their wide range of biological functions, including inhibition of platelet aggregation and antitumor activity. As a result, many studies have been conducted in an attempt to use these natural compounds as a basis for developing therapies for the treatment of various diseases. Furthermore, the FDA has approved Tirofiban and Eptifibatide as antiplatelet compounds, and they are synthesized from the structure of echistatin and barbourin, respectively. In this review, we discuss some of the main functional and structural characteristics of this class of proteins and their potential for therapeutic use. (AU)

FAPESP's process: 21/11936-3 - Center for Translational Science and Biopharmaceutical Development
Grantee:Benedito Barraviera
Support Opportunities: Research Grants - Science Centers for Development
FAPESP's process: 20/13176-3 - Human monoclonal antibodies (scFv) discovery with cross-reactivity and pH-dependent to metalloproteases from Bothrops spp
Grantee:Isadora Sousa de Oliveira
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 20/15670-5 - Isolation and functional and structural characterization of antitumor peptide from snake venoms of the Bothrops genre
Grantee:Gabriela de Oliveira Almeida
Support Opportunities: Scholarships in Brazil - Scientific Initiation
FAPESP's process: 22/08964-8 - Discovery of human monoclonal antibodies (scFv) with cross-reactivity and pH-dependent targeting metalloprotease from Bothrops spp.
Grantee:Isadora Sousa de Oliveira
Support Opportunities: Scholarships abroad - Research Internship - Post-doctor
FAPESP's process: 19/10173-6 - Production, modification and characterization of animal toxins with potential biotechnological application
Grantee:Eliane Candiani Arantes Braga
Support Opportunities: Regular Research Grants
FAPESP's process: 22/05554-3 - Bioprospection of low molecular weight compounds with antileukemic activity in Bothrops moojeni venom
Grantee:Gabriela de Oliveira Almeida
Support Opportunities: Scholarships in Brazil - Master
FAPESP's process: 22/04804-6 - Bioprospection of low molecular weight anticancer molecules from Bothrops genus snake venom
Grantee:Suely Vilela
Support Opportunities: BIOTA-FAPESP Program - Regular Research Grants