A Disintegrin from the Venom of Bothrops colombiensis (Mapanare)

Elda E. Sánchez^1,2, Jacob A. Galán, Gonzalo López, Alexis Rodríguez-Acosta² and John C. Pérez¹

1 Natural Toxins Research Center (NTRC), Texas A&M University-Kingsville, MSC 158, Kingsville, TX 78363, 2 Universidad Central de Venezuela, Instituto de Medicina Tropical, Sección de Inmunoquímica, Caracas 1041, Venezuela

Snake venoms contain over 300 different types of proteins that aid in the capture and the digestion of prey.  Many of these proteins have enzymatic activity while others are non-enzymatic.  Synergistically these proteins work to break down tissue causing detrimental affects, but individually some of these proteins could serve in the treatment of heart attacks, strokes and cancers.  Disintegrins are non-enzymatic, low molecular weight, peptides that affect cell-cell and cell-matrix interactions by binding to integrins found on the surfaces of various cells.  There are over 90 disintegrins that have been isolated from snake venom which carry out similar activities but with different efficiencies on different types of cells (e.g. platelets, cancer cells).  In this study, a disintegrin has been isolated from the venom of Bothropscolombiensis (BC-12) by reverse phase C18 and size exclusion chromatography. The calculated pI was 5.74 and the molecular mass was determined to be 7.7 kDa by matrix assisted laser desorption ionization time-of-flight, time-of-flight mass spectrometry (MALDI TOF-TOF).  BC-12 showed 68% homology with the disintegrin cotiarin isolated from the venom B. cotiara.  BC-12 inhibited ADP-induced platelet aggregation in whole blood by a Chrono-Log Aggregometer. BC-12 was also able to inhibit tumor cell (T24, human urinary bladder carcinoma) adhesion to fibronectin in a dose dependant manner.

Correspondence to: elda.sanchez@tamuk.edu