Conformational investigation of peptides using solid-state NMR spectroscopy—A study of polymorphism of β-turn peptides containing diprolines

Yarava, JR and Nishiyama, Y and Raghothama, S and Ramanathan, KV (2020) Conformational investigation of peptides using solid-state NMR spectroscopy—A study of polymorphism of β-turn peptides containing diprolines. In: Chemical Biology and Drug Design, 95 (3). pp. 394-407.

PDF che_bio_dru_90-3_394-407_2020.pdf - Published Version Restricted to Registered users only Download (2MB) | Request a copy

Abstract

The construction of complex protein folds relies on the precise conversion of a linear polypeptide chain into a compact 3-dimensional structure. In this context, study of isolated secondary structural modules containing short stretches of amino acids assumes significance. Additionally, peptides, both natural and synthetic, play a major role as potential drugs. With a view to understand the local conformations adopted by peptides in the solid state, we propose a multinuclear NMR approach utilizing spectra of nuclei in their natural isotopic abundance. Various solid-state NMR experiments have been utilized for assignment of the spectra. Additionally, the gauge-including projector augmented-wave (GIPAW) calculations were used to confirm the assignments. Particularly, the utility of the double-quantum–single-quantum correlation experiments is highlighted for the purpose of assignment and for inferring the conformation across the peptide bond. The methodology is illustrated for the case of designed peptides containing diproline residues occurring at the β-turns for identifying their cis-trans conformational polymorphism. The proposed method promises to be of use in the study of conformations of small- to medium-sized peptides such as antimicrobial peptides and in the study of polymorphism leading to applications in drug development protocols

Item Type:	Journal Article
Publication:	Chemical Biology and Drug Design
Publisher:	Blackwell Publishing Ltd
Additional Information:	The copyright for this article belongs to the Blackwell Publishing Ltd
Keywords:	peptide; polypeptide antibiotic agent; proline; peptide, amino terminal sequence; Article; calculation; carbon nuclear magnetic resonance; drug design; heteronuclear multiple quantum coherence; heteronuclear single quantum coherence; molecular interaction; nuclear magnetic resonance spectroscopy; priority journal; protein conformation; protein polymorphism; protein secondary structure; proton nuclear magnetic resonance; solid state; amino acid sequence; chemistry; crystallization; molecular model; nuclear magnetic resonance spectroscopy; protein conformation; structure activity relation, Amino Acid Sequence; Crystallization; Magnetic Resonance Spectroscopy; Models, Molecular; Peptides; Proline; Protein Conformation; Structure-Activity Relationship
Department/Centre:	Division of Chemical Sciences > NMR Research Centre (Formerly Sophisticated Instruments Facility) Division of Physical & Mathematical Sciences > Physics
Date Deposited:	02 Feb 2023 05:08
Last Modified:	02 Feb 2023 05:08
URI:	https://eprints.iisc.ac.in/id/eprint/79706

Actions (login required)

View Item