A ∩ of 2C3*
*A Union of Two Catalog Core Competencies (With apologies to mathematical accuracy for the sake of literary license).
Typically, we cover either venoms or RGD peptides in our PepTalk, but in this case we are looking at a unique intersectional space for them. Viper venoms contain several components, many of which are proteins or peptides. One such group is the disintegrins. Disintegrins are disulfide-rich and prevent fibrinogen bonding and subsequent platelet aggregation by binding to the αIIbβ3 receptor.1 They contain the Arg-Gly-Asp (RGD) or Lys-Gly-Asp (KGD) sequence, which is of importance for binding to the RGD-integrins. This sequence is a cell attachment site for many proteins and are involved in many cell processes, including cell proliferation and differentiation.2
In a new paper, published in Toxins, scientists look at the potential for snake venom disintegrins as an antithrombotic treatment. Thrombosis is the formation of blood clots within a blood vessel. This process can be dangerous with a need to prevent thrombosis, leading to favorable cardiovascular outcomes.
However, traditional antithrombotics can cause dangerous extraneous bleeding. Kuo et al., report that integrin conformational changes seem to be the cause. They looked at new RGD peptides derived from snake venom that do not cause these conformational changes and, therefore, do not increase bleeding risk.3 This new approach may lead to the development of safer and equally effective antithrombosis treatments.
1. M. Pennington, et al., Bioorganic & Medicinal Chemistry, 26(10), 2738 (2018).
3. Yu-Ju Kuo, Ching-Hu Chung, & Tur-Fu Huang, Toxins, 11(7), 372 (2019).