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Structure-activity relationships of C-terminal tri- and tetrapeptide fragments that inhibit gastrin activity

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 c...

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Published in:	Journal of medicinal chemistry 1985-03, Vol.28 (3), p.273-278
Main Authors:	Martinez, Jean, Bali, Jean Pierre, Magous, Richard, Laur, Janine, Lignon, Marie Francoise, Briet, Christian, Nisato, Dino, Castro, Bertrand
Format:	Article
Language:	English
Subjects:	acids Animals Biological and medical sciences Chemical Phenomena Chemistry Gastric Acid - metabolism gastric mucosa gastrin Gastrins - antagonists & inhibitors General pharmacology Medical sciences Oligopeptides - pharmacology Peptide Fragments - pharmacology peptide synthesis Pharmacology. Drug treatments Physicochemical properties. Structure-activity relationships Rats Structure-Activity Relationship
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cited_by	cdi_FETCH-LOGICAL-a329t-1cf84a433a8712c277ce7fcbe706c713b84e1b9408d0ab5ef97320d36fb76e743
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container_end_page	278
container_issue	3
container_start_page	273
container_title	Journal of medicinal chemistry
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creator	Martinez, Jean Bali, Jean Pierre Magous, Richard Laur, Janine Lignon, Marie Francoise Briet, Christian Nisato, Dino Castro, Bertrand
description	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.
doi_str_mv	10.1021/jm00381a002
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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. 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Med. Chem</addtitle><description>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.</description><subject>acids</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Gastric Acid - metabolism</subject><subject>gastric mucosa</subject><subject>gastrin</subject><subject>Gastrins - antagonists & inhibitors</subject><subject>General pharmacology</subject><subject>Medical sciences</subject><subject>Oligopeptides - pharmacology</subject><subject>Peptide Fragments - pharmacology</subject><subject>peptide synthesis</subject><subject>Pharmacology. Drug treatments</subject><subject>Physicochemical properties. 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Med. Chem</addtitle><date>1985-03</date><risdate>1985</risdate><volume>28</volume><issue>3</issue><spage>273</spage><epage>278</epage><pages>273-278</pages><issn>0022-2623</issn><eissn>1520-4804</eissn><coden>JMCMAR</coden><notes>istex:A0747FC00DA756EED186D4F0346AC373C22A1AD8</notes><notes>ark:/67375/TPS-W0S257MP-V</notes><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>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.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>3973899</pmid><doi>10.1021/jm00381a002</doi><tpages>6</tpages></addata></record>
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subjects	acids Animals Biological and medical sciences Chemical Phenomena Chemistry Gastric Acid - metabolism gastric mucosa gastrin Gastrins - antagonists & inhibitors General pharmacology Medical sciences Oligopeptides - pharmacology Peptide Fragments - pharmacology peptide synthesis Pharmacology. Drug treatments Physicochemical properties. Structure-activity relationships Rats Structure-Activity Relationship
title	Structure-activity relationships of C-terminal tri- and tetrapeptide fragments that inhibit gastrin activity
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