Detail of "4302-66-3"

Reference

Structure-function studies of N-acyl derivatives of tryptophan that function as specific cholecystokinin receptor antagonists

Structure-function studies of N-acyl derivatives of tryptophan that function as specific cholecystokinin receptor antagonists. Jensen, Robert T.; Jones, Susanna W.; Gardner, Jerry D. (Dig. Dis. Branch, Natl. Inst. Arthritis, Diabetes, Dig. Kidney Dis., Bethesda, MD 20205, USA). Biochim. Biophys. Acta, 761(3), 269-77 (English) 1983. CODEN: BBACAQ. ISSN: 0006-3002. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) L-Tryptophan [73-22-3], D-tryptophan [153-94-6] and each N-acyl deriv. tested inhibited cholecystokinin [9011-97-6]-stimulated amylase secretion and outflux of 45Ca by dispersed pancreatic acini, and there was a good correlation between the ability of a particular agent to inhibit the action of cholecystokinin on acinar function and its ability to inhibit binding of 125I-labeled cholecystokinin to pancreatic acini. The inhibition of the action of cholecystokinin caused by L-tryptophan and various acyl derivs. was specific, competitive, and fully reversible. In functioning as a cholecystokinin receptor antagonist, the relative potencies of the agents tested were: carbobenzoxy-L-tryptophan [7432-21-5] > benzotript [39544-74-6] > N-benzoyl-L-tryptophan [4302-66-3] = N-tert-butyloxycarbonyl-L-tryptophan [13139-14-5] > acetyl-L-tryptophan [1218-34-4] > L-tryptophan. In inhibiting the actions of cholecystokinin, native as well as N-acyl derivs. of D-tryptophan were euipotent with the corresponding compd. contg. L-tryptophan. L-Phenylalanine [63-91-2], L-methionine [63-68-3], or L-aspartic acid [56-84-8] did not alter the action of cholecystokinin on pancreatic acini. The antagonism of the actions of cholecystokinin was not restricted to N-acyl derivs. 2488-15-5 and 153-94-6 which are cas registry numbers of substances are two of reagents here. of L-tryptophan because N-tert-butyloxycarbonyl-L-methionine [2488-15-5] and N-tert-butyloxycarbonyl-L-phenylalanine [13734-34-4], but not N-tert-butyloxycarbonyl-L-aspartic acid [13726-67-5] also antagonized the actions of cholecystokinin. Both the nature of the N-acyl group and the amino acid residue appear to be important determinants of the affinity of the antagonist for the cholecystokinin receptor. For derivs. of L-tryptophan, the more hydrophobic the N-acyl moiety, the greater the affinity of the deriv. for the cholecystokinin receptor. .