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Natural Abundant Solid State NMR Studies in Designed Tripeptides for Differentiation of Multiple Conformers

Jayanthi, S and Chatterjee, Bhaswati and Raghothama, S (2009) Natural Abundant Solid State NMR Studies in Designed Tripeptides for Differentiation of Multiple Conformers. In: Biopolymers, 91 (10). pp. 851-860.

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Official URL: http://www3.interscience.wiley.com/journal/1224682...


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 C-13 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-beta and C-gamma carbon of Proline in peptide (1) both in solution and SSNMR. Peptide (2) and (3) provided single set of resonances which represented all transform across the di-Proline segment. The results are In agreement with the X-ray analysis. Solid state N-15 resonances, especially from Proline residues provided additional information, which is normally not observable in solution state NMR. H-1 chemical shifts are also obtained from a two-dimensional heteronuclear correlation experiment between H-1-C-13. The results confirm the utility of NMR as a useful tool for identifying different conformers in peptides in the solid state. (C) 2009 Wiley Periodicals, Inc. Biopolymers 91: 851-860, 2009.

Item Type: Journal Article
Publication: Biopolymers
Publisher: John Wiley and Sons
Additional Information: Copyright of this article belongs to John Wiley and Sons.
Keywords: solid state NMR;multiple conformers;designed peptided containing Prolines.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Division of Chemical Sciences > NMR Research Centre (Formerly Sophisticated Instruments Facility)
Division of Physical & Mathematical Sciences > Physics
Date Deposited: 15 Dec 2009 10:18
Last Modified: 19 Sep 2010 05:45
URI: http://eprints.iisc.ac.in/id/eprint/23286

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