Photochemically-Activated Probes of Protein−Protein Interactions
- 17 May 2007
- journal article
- letter
- Published by American Chemical Society (ACS) in Organic Letters
- Vol. 9 (12) , 2249-2252
- https://doi.org/10.1021/ol070238t
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.Keywords
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