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Theoretical and NMR Conformational Studies of β-Proline Oligopeptides With Alternating Chirality of Pyrrolidine Units.

Theoretical and NMR Conformational Studies of β-Proline Oligopeptides With Alternating Chirality of Pyrrolidine Units.

Authors :
Mantsyzov AB
Savelyev OY
Ivantcova PM
Bräse S
Kudryavtsev KV
Polshakov VI
Source :
Frontiers in chemistry [Front Chem] 2018 Mar 28; Vol. 6, pp. 91. Date of Electronic Publication: 2018 Mar 28 (Print Publication: 2018).
Publication Year :
2018

Abstract

Synthetic β-peptides are potential functional mimetics of native α-proteins. A recently developed, novel, synthetic approach provides an effective route to the broad group of β-proline oligomers with alternating patterns of stereogenic centers. Conformation of the pyrrolidine ring, Z / E isomerism of β-peptide bonds, and hindered rotation of the neighboring monomers determine the spatial structure of this group of β-proline oligopeptides. Preferences in their structural organization and corresponding thermodynamic properties are determined by NMR spectroscopy, restrained molecular dynamics and quantum mechanics. The studied β-proline oligopeptides exist in dimethyl sulfoxide solution in a limited number of conformers, with compatible energy of formation and different spatial organization. In the β-proline tetrapeptide with alternating chirality of composing pyrrolidine units, one of three peptide bonds may exist in an E configuration. For the alternating β-proline pentapeptide, the presence of an E configuration for at least of one β-peptide bond is mandatory. In this case, three peptide bonds synchronously change their configurations. Larger polypeptides may only exist in the presence of several E configurations of β-peptide bonds forming a wave-like extended structure.

Details

Language :
English
ISSN :
2296-2646
Volume :
6
Database :
MEDLINE
Journal :
Frontiers in chemistry
Publication Type :
Academic Journal
Accession number :
29644215
Full Text :
https://doi.org/10.3389/fchem.2018.00091