Unknown

Dataset Information

0

Photochemically-activated probes of protein-protein interactions.


ABSTRACT: The activity of light-activatable ("caged") compounds can be temporally and spatially controlled, thereby providing a means to interrogate intracellular biochemical pathways as a function of time and space. Nearly all caged peptides contain photocleavable groups positioned on the side chains of key residues. We describe an alternative active site targeted strategy that disrupts the interaction between the protein target (SH2 domain, kinase, and proteinase) and a critical amide NH moiety of the peptide probe.

SUBMITTER: Nandy SK 

PROVIDER: S-EPMC3057037 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Photochemically-activated probes of protein-protein interactions.

Nandy Sandip K SK   Agnes Richard S RS   Lawrence David S DS  

Organic letters 20070517 12


The activity of light-activatable ("caged") compounds can be temporally and spatially controlled, thereby providing a means to interrogate intracellular biochemical pathways as a function of time and space. Nearly all caged peptides contain photocleavable groups positioned on the side chains of key residues. We describe an alternative active site targeted strategy that disrupts the interaction between the protein target (SH2 domain, kinase, and proteinase) and a critical amide NH moiety of the p  ...[more]

Similar Datasets

| S-EPMC7909741 | biostudies-literature
| S-EPMC7949286 | biostudies-literature
| S-EPMC9828268 | biostudies-literature
| S-EPMC2741162 | biostudies-other
| S-EPMC1137768 | biostudies-other
| S-EPMC2879513 | biostudies-literature
| S-EPMC9977449 | biostudies-literature
| S-EPMC3587108 | biostudies-literature
| S-EPMC8259317 | biostudies-literature
| S-EPMC5382698 | biostudies-literature