Antidiuretic and pressor activities of vasopressin analogs with L‐alaninamide and D‐alaninamide substitutions at position 9

Angeliki Buku, Diana Gazis, Irving L. Schwartz

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

Analogs of arginine vasopressin (AVP) and lysine vasopressin (LVP) — with an L‐alaninamide residue or a D‐alaninamide residue replacing the naturally occurring glycinamide in position 9 — lose virtually all pressor activity but retain from 10 to 70% of the antidiuretic activity of their parent hormones. These findings, in conjunction with the data of others on the biological consequences of alterations in positions 7 and 8, show that the antidiuretic receptor will tolerate considerably more structural alteration in the C‐terminal tripeptide “tail” of the vasopressins than will the pressor receptor.

Original languageEnglish
Pages (from-to)551-557
Number of pages7
JournalInternational Journal of Peptide and Protein Research
Volume23
Issue number5
DOIs
StatePublished - May 1984

Keywords

  • alaninamide substitution
  • antidiuretic activity
  • peptide hormones
  • peptide synthesis
  • pressor activity
  • receptor selectivity
  • structure vs. activity
  • vasopressin analogs
  • vasopressin receptors

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