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Conformation and chiral effects in α,β,α-tripeptides

AuthorsSaavedra, Carlos J.; Boto, Alicia ; Hernández, Rosendo ; Miranda, José Ignacio; Aizpurua, Jesús M.
Peptides and proteins
Molecular structure
Issue Date5-Jul-2012
PublisherAmerican Chemical Society
CitationJournal of Organic Chemistry 77(14): 5907-5913 (2012)
AbstractShort α,β,α-tripeptides comprising a central chiral trisubstituted β 2,2,3*-amino acid residue form unusual γ-turns and δ-turns in CDCl 3 and DMSO-d 6 solutions but do not form β-turns. Thermal coefficients of backbone amide protons, 2D-NMR spectra, and molecular modeling revealed that these motifs were strongly dependent on the configuration (chiral effect) of the central β-amino acid residue within the triad. Accordingly, SSS tripeptides adopted an intraresidual γ-turn like (C6) arrangement in the central β-amino acid, whereas SRS diastereomers preferred an extended δ-turn (C9) conformation. A different SRS-stabilizing bias was observed in the crystal structures of the same compounds, which shared the extended δ-turn (C9) found in solution, but incorporated an additional extended β-turn (C11) to form an overlapped double turn motif.
Publisher version (URL)http://dx.doi.org/10.1021/jo300892u
Identifiersdoi: 10.1021/jo300892u
issn: 0022-3263
e-issn: 1520-6904
Appears in Collections:(IPNA) Artículos
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