Binding dynamics of a stapled peptide targeting the transcription factor NF-Y

In this study, we investigate how truncated stapled α-helical peptides interact with the transcription factor Nuclear Factor-Y (NF-Y). We identified a 13-mer minimal binding core region, for which two crystal structures with an altered C-terminal peptide conformation when bound to NF-Y were obtained. Subsequent molecular dynamics simulations confirmed that the C-terminal part of the stapled peptide is indeed relatively flexible while still showing defined interactions with NF-Y. Our findings highlight the importance of flexibility in the bound state of peptides, which can contribute to overall binding affinity.PMID:38470946 | DOI:10.1002/cbic.202400020

Source: Chembiochem - March 12, 2024 Category: Biochemistry Authors: Canan Durukan Federica Arbore Rasmus Klintrot Carlo Bigiotti Ioana M Ilie Jocelyne Vreede Tom N Grossmann Sven Hennig Source Type: research