Conformational effects of the non-natural alpha-methylserine on small peptides and glycopeptides

  1. Fernández-Tejada, A. 1
  2. Corzana, F. 1
  3. Busto, J.H. 1
  4. Avenoza, A. 1
  5. Peregrina, J.M. 1
  1. 1 Universidad de La Rioja

    Universidad de La Rioja

    Logroño, España

    GRID grid.119021.a

Journal of Organic Chemistry

ISSN: 0022-3263

Year of publication: 2009

Volume: 74

Issue: 24

Pages: 9305-9313

Type: Article

Export: RIS
DOI: 10.1021/jo901988w PMID: 19924838 SCOPUS: 2-s2.0-73149103487 WoS: 000272462100007 GOOGLE SCHOLAR


Cited by

  • Scopus Cited by: 13 (12-06-2021)

Journal Citation Reports

  • Year 2009
  • Journal Impact Factor: 4.219
  • Best Quartile: Q1
  • Area: CHEMISTRY, ORGANIC Quartile: Q1 Rank in area: 8/57 (Ranking edition: SCIE)

SCImago Journal Rank

  • Year 2009
  • SJR Journal Impact: 2.198
  • Best Quartile: Q1
  • Area: Organic Chemistry Quartile: Q1 Rank in area: 15/169


(Chemical Equation Presented) The synthesis and the conformational analysis in aqueous solution of a peptide and a glycopeptide containing the sequence threonine-alanine-alanine (Thr-Ala-Ala) are reported. Furthermore, the threonine residue has been replaced by the quaternary amino acid α-methylserine (MeSer) and their corresponding non-natural peptide and glycopeptide are also studied. The conformational analysis in aqueous solution combines NOEs and coupling constants data with Molecular Dynamics (MD) simulations with time-averaged restraints. The study reveals that the β-O-glycosylation produces a remarkable and completely different effect on the backbone of the peptide derived from Thr and MeSer. In the former, the β-O-glycosylation is responsible for the experimentally observed shift from extended conformations (peptide) to folded ones (glycopeptide). In contrast, the β-O-glycosylation of the MeSer-containing peptide, which clearly shows two main conformations in aqueous solution [extended ones (70%) and β-turn (30%)], causes a high degree of flexibility for the backbone. © 2009 American Chemical Society.