Synthesis and sst2 binding profiles of new [Tyr3]octreotate analogs

✍ Scribed by Christos Petrou; Vassiliki Magafa; Anastasia Nikolopoulou; George Pairas; Berthold Nock; Theodosia Maina; Paul Cordopatis

• Book ID: 105360802
• Publisher: John Wiley and Sons
• Year: 2008
• Tongue: English
• Weight: 109 KB
• Volume: 14
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.989

✦ Synopsis

Abstract

One of the main objectives of our current work is the development of new somatostatin analogs that would retain the general characteristics of [Tyr^3^]octreotate (Tate) while showing potential for clinical application. In this respect, study of their interaction with the sst~2~ is crucial in providing preliminary structure‐activity relationships data. In the present work we report on the synthesis and the preliminary biological evaluation of a total of 15 new structurally modified [Tyr^3^]octreotate analogs. The binding affinities were determined during competition binding assays in sst~2~‐positive rat acinar pancreatic AR4‐2J cell membranes using [^125^I‐Tyr^3^]octreotide as the radioligand. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.