Specific, covalent binding of an azidoretinoid to cellular retinoic acid-binding protein.
Two C(5)-azido substituted aromatic retinoids were evaluated as photoaffinity probes for studying the mechanism of retinoid action. The secondary azide 1 and the tertiary azide 2 were equipotent with the parent C(5)-geminal-dimethyl substituted aromatic retinoid 3 in stimulating F9-cell differentiation. Both azides bound covalently to cellular retinoic acid-binding protein upon photolysis, but the secondary azide was twice as efficient, likely because of lesser steric hindrance. The covalent binding of azide 1 was specific, since it was inhibited by retinoic acid. Thus substitution of a photolabile group onto aromatic retinoids does not abolish biological activity and affinity for cellular retinoic acid-binding protein.
D000345:Affinity Labels; D000818:Animals; D001386:Azides / Q000378:metabolism* / Q000494:pharmacology; D002352:Carrier Proteins / Q000378:metabolism*; D002454:Cell Differentiation / Q000187:drug effects; D002460:Cell Line; D007797:Laminin / Q000096:biosynthesis; D010777:Photochemistry; D018168:Receptors, Retinoic Acid; D012176:Retinoids / Q000378:metabolism* / Q000494:pharmacology; D013724:Teratoma / Q000473:pathology
D000345:Affinity Labels; D001386:Azides; D002352:Carrier Proteins; D007797:Laminin; D018168:Receptors, Retinoic Acid; D012176:Retinoids; C048125:6-(5-azido-5,6,7,8-tetrahydro-8,8-dimethyl-2-naphthalenyl)-2-naphthalenecarboxylic acid; C048126:6-(5-azido-5,6,7,8-tetrahydro-5,8,8-trimethyl-2-naphthalenyl)-2-naphthalenecarboxylic acid