Martinez J, Bali J P, Magous R, Laur J, Lignon M F, Briet C, Nisato D, Castro B
J Med Chem. 1985 Mar;28(3):273-8. doi: 10.1021/jm00381a002.
A series of tri- and tetrapeptide derivatives, analogues of the gastrin C-terminal region with no phenylalanine residue, were synthesized. These peptides were tested for their ability to inhibit gastrin-stimulated acid secretion in vivo as well as binding of [125I]-(Nle11)-HG-13 to gastric mucosal cell receptors in vitro. Most of the peptides tested exhibited gastrin antagonist activity in vivo and in vitro. Most active derivatives were 20-30 times more potent than the well-known gastrin antagonist derivatives proglumide and benzotript and had 20-200 times more binding affinity. The smallest fragment exhibiting antagonist activity was the tripeptide Boc-L-tryptophyl-L-methionyl-L-aspartic acid amide.
合成了一系列三肽和四肽衍生物，它们是胃泌素C末端区域的类似物，且不含苯丙氨酸残基。对这些肽进行了测试，以考察它们在体内抑制胃泌素刺激的胃酸分泌的能力，以及在体外与胃黏膜细胞受体结合[125I]-(Nle11)-HG-13的能力。大多数测试的肽在体内和体外均表现出胃泌素拮抗剂活性。最具活性的衍生物比著名的胃泌素拮抗剂衍生物丙谷胺和苯曲磷酯效力高20 - 30倍，且结合亲和力高20 - 200倍。表现出拮抗剂活性的最小片段是三肽Boc-L-色氨酰-L-甲硫氨酰-L-天冬氨酸酰胺。
