Synthesis and conformational studies of novel cyclic peptides constrained into a 3 10 helical structure by a heterochiral D-pro-L-pro dipeptide template
Related Experiment Video
Updated: Aug 25, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
Published on: August 1, 2018
I Nageshwara Rao1, Anima Boruah, S Kiran Kumar
1Dr. Reddy's Laboratories, Discovery Research, Bollaram Road, Miyapur, Hyderabad 500 050, India.
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.
Related Concept Videos
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Organization
Protein Organization
The primary structure of a protein is its amino acid sequence.
Peptide Bonds
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...

