Photoinduced reconfiguration to control the protein-binding affinity of azobenzene-cyclized peptides.

ABSTRACT: The impact of next-generation biorecognition elements (ligands) will be determined by the ability to remotely control their binding activity for a target biomolecule in complex environments. Compared to conventional mechanisms for regulating binding affinity (pH, ionic strength, or chaotropic agents), light provides higher accuracy and rapidity, and is particularly suited for labile targets. In this study, we demonstrate a general method to develop azobenzene-cyclized peptide ligands with light-controlled affinity for target proteins. Light triggers a cis/trans isomerization of the azobenzene, which results in a major structural rearrangement of the cyclic peptide from a non-binding to a binding configuration. Critical to this goal are the ability to achieve efficient photo-isomerization u

SUBMITTER: Day K 

PROVIDER: S-EPMC7945681 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature