Photochemically-activated probes of protein-protein interactions.
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.
Nandy
Sandip K
SK
Department of Biochemistry, The Albert Einstein College of Medicine of Yeshiva University, 1300 Morris Park Avenue, Bronx, New York 10461-1602, USA.
Agnes
Richard S
RS
Lawrence
David S
DS
D001665:Binding Sites; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry / Q000187:drug effects; D008027:Light; D008958:Models, Molecular; D015394:Molecular Structure; D015345:Oligonucleotide Probes / Q000737:chemistry* / Q000494:pharmacology / Q000528:radiation effects; D010447:Peptide Hydrolases / Q000737:chemistry / Q000187:drug effects; D010766:Phosphorylation; D010777:Photochemistry; D011485:Protein Binding; D012680:Sensitivity and Specificity; D013329:Structure-Activity Relationship; D013997:Time Factors; D018909:src Homology Domains / Q000187:drug effects
D015345:Oligonucleotide Probes; D017868:Cyclic AMP-Dependent Protein Kinases; D010447:Peptide Hydrolases