Theoretical and NMR Conformational Studies of β-Proline Oligopeptides With Alternating Chirality of Pyrrolidine Units
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...
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| Format: | Article |
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Frontiers Media S.A.
2018-03-01
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| Series: | Frontiers in Chemistry |
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| Online Access: | http://journal.frontiersin.org/article/10.3389/fchem.2018.00091/full |
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| author | Alexey B. Mantsyzov Oleg Y. Savelyev Polina M. Ivantcova Stefan Bräse Stefan Bräse Konstantin V. Kudryavtsev Konstantin V. Kudryavtsev Vladimir I. Polshakov |
| author_facet | Alexey B. Mantsyzov Oleg Y. Savelyev Polina M. Ivantcova Stefan Bräse Stefan Bräse Konstantin V. Kudryavtsev Konstantin V. Kudryavtsev Vladimir I. Polshakov |
| author_sort | Alexey B. Mantsyzov |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-13T02:14:11Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 2296-2646 |
| language | English |
| last_indexed | 2024-04-13T02:14:11Z |
| publishDate | 2018-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Chemistry |
| spelling | doaj.art-d872ab658dee42c6815dcaaa041923a82022-12-22T03:07:12ZengFrontiers Media S.A.Frontiers in Chemistry2296-26462018-03-01610.3389/fchem.2018.00091327715Theoretical and NMR Conformational Studies of β-Proline Oligopeptides With Alternating Chirality of Pyrrolidine UnitsAlexey B. Mantsyzov0Oleg Y. Savelyev1Polina M. Ivantcova2Stefan Bräse3Stefan Bräse4Konstantin V. Kudryavtsev5Konstantin V. Kudryavtsev6Vladimir I. Polshakov7Faculty of Fundamental Medicine, M.V. Lomonosov Moscow State University, Moscow, RussiaFaculty of Fundamental Medicine, M.V. Lomonosov Moscow State University, Moscow, RussiaDepartment of Chemistry, M.V. Lomonosov Moscow State University, Moscow, RussiaInstitute of Organic Chemistry, Karlsruhe Institute of Technology, Karlsruhe, GermanyInstitute of Toxicology and Genetics, Karlsruhe Institute of Technology, Eggenstein-Leopoldshafen, GermanyDepartment of Chemistry, M.V. Lomonosov Moscow State University, Moscow, RussiaInstitute of Physiologically Active Compounds, Russian Academy of Sciences, Chernogolovka, RussiaFaculty of Fundamental Medicine, M.V. Lomonosov Moscow State University, Moscow, RussiaSynthetic 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.http://journal.frontiersin.org/article/10.3389/fchem.2018.00091/fullβ-peptidesfoldingNMR spectroscopysolution structurerestrained molecular dynamicsdensity functional theory (DFT) calculations |
| spellingShingle | Alexey B. Mantsyzov Oleg Y. Savelyev Polina M. Ivantcova Stefan Bräse Stefan Bräse Konstantin V. Kudryavtsev Konstantin V. Kudryavtsev Vladimir I. Polshakov Theoretical and NMR Conformational Studies of β-Proline Oligopeptides With Alternating Chirality of Pyrrolidine Units Frontiers in Chemistry β-peptides folding NMR spectroscopy solution structure restrained molecular dynamics density functional theory (DFT) calculations |
| title | Theoretical and NMR Conformational Studies of β-Proline Oligopeptides With Alternating Chirality of Pyrrolidine Units |
| title_full | Theoretical and NMR Conformational Studies of β-Proline Oligopeptides With Alternating Chirality of Pyrrolidine Units |
| title_fullStr | Theoretical and NMR Conformational Studies of β-Proline Oligopeptides With Alternating Chirality of Pyrrolidine Units |
| title_full_unstemmed | Theoretical and NMR Conformational Studies of β-Proline Oligopeptides With Alternating Chirality of Pyrrolidine Units |
| title_short | Theoretical and NMR Conformational Studies of β-Proline Oligopeptides With Alternating Chirality of Pyrrolidine Units |
| title_sort | theoretical and nmr conformational studies of β proline oligopeptides with alternating chirality of pyrrolidine units |
| topic | β-peptides folding NMR spectroscopy solution structure restrained molecular dynamics density functional theory (DFT) calculations |
| url | http://journal.frontiersin.org/article/10.3389/fchem.2018.00091/full |
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