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Characterization of the New Photoaffinity Probe (Bz 2 ‐K 24 )‐VIP
Author(s) -
TAN YOSSANVAR,
COUVINEAU ALAIN,
LACAPERE JEAN JACQUES,
LABURTHE MARC
Publication year - 2006
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1317.084
Subject(s) - characterization (materials science) , chemistry , radiochemistry , materials science , nanotechnology
Site‐directed mutagenesis and molecular modeling demonstrated that the N‐terminal ectodomain of the VPAC1 receptor is a major site of vasoactive intestinal peptide (VIP) binding. Previous studies with the [Bpa 6 ]‐VIP and [Bpa 22 ]‐VIP probes (substitution with the photoactivable Bpa for the residues 6 and 22 in VIP) showed spatial approximation between the amino acids 6 and 22 of VIP and the 104‐108 and 109‐119 sequences within the N‐terminal ectodomain of the receptor, respectively. Here, we characterize the new probe (Bz 2 ‐K 24 )‐VIP (substitution with the photoreactive Bz 2 ‐K for the residue 24 in VIP). After photolabeling and sequential digestions of the receptor, the 121‐133 sequence of the N‐terminal ectodomain was identified as the site of interaction. The N‐terminal ectodomain of the VPAC1 receptor is therefore an affinity trap for the central part of VIP, at least between residues 6 and 24.