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Natural abundant solid state NMR studies in designed tripeptides for differentiation of multiple conformers
Author(s) -
Jayanthi S.,
Chatterjee Bhaswati,
Raghothama S.
Publication year - 2009
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21270
Subject(s) - chemistry , tripeptide , conformational isomerism , solid state nuclear magnetic resonance , heteronuclear molecule , chatterjee , crystallography , carbon 13 nmr , peptide , two dimensional nuclear magnetic resonance spectroscopy , chemical shift , stereochemistry , nmr spectra database , molecule , nuclear magnetic resonance spectroscopy , spectral line , nuclear magnetic resonance , organic chemistry , biochemistry , physics , bengali , linguistics , philosophy , astronomy
Abstract Solid state NMR (SSNMR) experiments on heteronuclei in natural abundance are described for three synthetically designed tripeptides Piv‐ L Pro‐ L Pro‐ L Phe‐OMe ( 1 ), Piv‐ D Pro‐ L Pro‐ L Phe‐OMe ( 2 ), and Piv‐ D Pro‐ L Pro‐ L Phe‐NHMe ( 3 ). These peptides exist in different conformation as shown by solution state NMR and single crystal X‐ray analysis (Chatterjee et al., Chem Eur J 2008, 14, 6192). In this study, SSNMR has been used to probe the conformations of these peptides in their powder form. The 13 C spectrum of peptide ( 1 ) showed doubling of resonances corresponding to cis/cis form, unlike in solution where the similar doubling is attributed to cis/trans form. This has been confirmed by the chemical shift differences of C β and C γ carbon of Proline in peptide ( 1 ) both in solution and SSNMR. Peptide ( 2 ) and ( 3 ) provided single set of resonances which represented all trans form across the di‐Proline segment. The results are in agreement with the X‐ray analysis. Solid state 15 N resonances, especially from Proline residues provided additional information, which is normally not observable in solution state NMR. 1 H chemical shifts are also obtained from a two‐dimensional heteronuclear correlation experiment between 1 H 13 C. The results confirm the utility of NMR as a useful tool for identifying different conformers in peptides in the solid state. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 851–860, 2009. This article was originally published online as an accepted preprint. The “Published Online“ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com