Snake venom disintegrins update: insights about new findings

• Published in: Journal of Venomous Animals and Toxins including Tropical Diseases
• Main Authors: Gabriela de Oliveira Almeida, Isadora Sousa de Oliveira, Eliane Candiani Arantes, Suely Vilela Sampaio
• Format: Article in Journal/Newspaper
• Language: English
• Published: SciELO 2023
• Subjects: disintegrins; SVMP; ADAM; snake venom; integrins; RGD domain; Arctic medicine. Tropical medicine; RC955-962; Toxicology. Poisons; RA1190-1270; Zoology; QL1-991; Arctic
• Online Access: https://doi.org/10.1590/1678-9199-jvatitd-2023-0039; https://doaj.org/article/4e06ec9651264924843aa4ae7ff4a2c2

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.