Allosteric modulation of the dopamine receptor by conformationally constrained type VI β-turn peptidomimetics of Pro-Leu-Gly-NH2

Ashish P. Vartak, Kevin Skoblenick, Nancy Thomas, Ram K. Mishra, Rodney L. Johnson

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

A peptidomimetic of Pro-Leu-Pro-NH2, 7, possessing an indolizidinone type VI β-turn mimic was synthesized via improved high-yielding protocols for the preparation and Cbz protection of α-allylproline. Bicyclic peptidomimetic 7 and spirobicylic peptidomimetic 8 enhanced the binding of [3H]N-propylnorapomorphine to dopamine receptors indicating that a type VI β-turn is a possible bioactive conformation of the homochiral Pro-Leu-Pro-NH2 and Pro-Pro-Pro-NH2 analogues of Pro-Leu-Gly-NH2 at the dopamine receptor allosteric regulatory site.

Original languageEnglish (US)
Pages (from-to)6725-6729
Number of pages5
JournalJournal of Medicinal Chemistry
Volume50
Issue number26
DOIs
StatePublished - Dec 27 2007

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