A comparative study of two structurally related analogs of Asp1-Ile5-angiotensin II

Türker R., Gündoǧan N.

Naunyn-Schmiedeberg's Archives of Pharmacology, vol.282, no.4, pp.411-420, 1974 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 282 Issue: 4
  • Publication Date: 1974
  • Doi Number: 10.1007/bf00500989
  • Journal Name: Naunyn-Schmiedeberg's Archives of Pharmacology
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Agricultural & Environmental Science Database, BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Chimica, EMBASE, MEDLINE, Veterinary Science Database
  • Page Numbers: pp.411-420
  • Keywords: (N,N-Dimethyl) Gly1-Ile5-Ile8-Angiotensin II, Asp1-β-Amid-Val5-Angiotensin II, Competitive Antagonism, Sar1-Ile5-Ile8-Angiotensin II
  • Ankara University Affiliated: Yes

Abstract

Two new synthetic analogs of Asp1-Ile5-angiotensin II, Sar1-Ile5-Ile8-angiotensin II and (N,N-dimethyl) Gly1-Ile5-Ile8-angiotensin II which are chemically related, have a potent competitive antagonistic action against Asp1-β-amid-Val5-angiotensin II on the rabbit isolated aorta, rat ascending colon, isolated perfused heart of cat and in vivo on the blood pressure and intestinal motility of the chloralose-anesthetized cat. Compared to Sar1-Ile5-Ile8-angiotensin II, (N,N-dimethyl) Gly1-Ile5-Ile8-angiotensin II has equal antagonistic potency on the isolated preparations but a lower potency in vivo. The duration of the antagonistic effect of (N,N-dimethyl) Gly1-Ile5-Ile8-angiotensin II in all preparations investigated has been found to be significantly shorter than that of Sar1-Ile5-Ile8-angiotensin II. It is assumed that replacement of sarcosine with N,N-dimethyl glycine at the NH2-terminal position, enhances the degradation of the analog by aminopeptidase and therefore decreases its half-life. © 1974 Springer-Verlag.