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Title: Synthesis and conformational studies of novel cyclic peptides constrained into a 3 10 helical structure by a heterochiral D-pro-L-pro dipeptide template. Author: Rao IN, Boruah A, Kumar SK, Kunwar AC, Devi AS, Vyas K, Ravikumar K, Iqbal J. Journal: J Org Chem; 2004 Mar 19; 69(6):2181-4. PubMed ID: 15058968. Abstract: An acyclic tripeptide based on a heterochiral D-pro-L-pro template shows a propensity to exist as a 3(10) helical conformation and can be cyclized, via ring-closing metathesis, to the corresponding cyclic tetrapeptides without disrupting the helical conformations in CDCl(3) as well as in DMSO-d(6) solutions. The detailed conformational studies were carried out by using NMR spectroscopy, X-ray crystallography, molecular dynamic simulations, and circular dichroism spectroscopy.[Abstract] [Full Text] [Related] [New Search]