Role of single disulfide linkages in the folding and activity of scyllatoxin ‐based BH3 domain mimetics

This study underscores the importance of structural dynamics in BH3:Bcl‐2 interactions and further validates ScTx‐based ligands as potential modulators of anti‐apoptotic Bcl‐2 function. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.

Structural variants of synthetic peptides based on scyllatoxin (ScTx) designed to mimic the helical BH3 interaction domain of the pro‐apoptotic Bcl‐2 protein Bax were developed and the contribution of single disulfides in the folding and function of ScTx‐Bax BH3 mimetics was investigated. It was dterminded that the position of the disulfide linkages had significant implications on the ability for ScTx‐Bax proteins to fold and target anti‐apoptotic Bcl‐2 proteins in vitro.

Source: Journal of Peptide Science - March 1, 2017 Category: Biochemistry Authors: Danushka Arachchige, M. Margaret Harris, Zachary Coon, Jacob Carlsen, Justin M. Holub Tags: Rapid Communication Source Type: research