(αMe)Hyv: chemo-enzymatic synthesis, and preparation and preferred conformation of model depsipeptidesElectronic supplementary information (ESI) available: analytical data. See http://www.rsc.org/suppdata/p2/b1/b107691b/
Peggion, Cristina; Barazza, Alessandra; Formaggio, Fernando; Crisma, Marco; Toniolo, Claudio; Villa, Marzia; Tomasini, Claudia; Mayrhofer, Herbert; Pöchlauer, Peter; Kaptein, Bernard; Broxterman, Quirinus B.; Peggion Cristina; Biopolymer Research Centre, CNR, Department of Organic Chemistry; Barazza Alessandra; Biopolymer Research Centre, CNR, Department of Organic Chemistry; Formaggio Fernando; Biopolymer Research Centre, CNR, Department of Organic Chemistry; Crisma Marco; Biopolymer Research Centre, CNR, Department of Organic Chemistry; Toniolo Claudio; Biopolymer Research Centre, CNR, Department of Organic Chemistry; Villa Marzia; Department of Chemistry â G. Ciamicianâ , University of Bologna; Tomasini Claudia; Department of Chemistry â G. Ciamicianâ , University of Bologna; Mayrhofer Herbert; DSM Fine Chemicals Austria, P.O. Box 933; Pöchlauer Peter; DSM Fine Chemicals Austria, P.O. Box 933; Kaptein Bernard; DSM Fine Chemicals, Advanced Synthesis and Catalysis; Broxterman Quirinus B.; DSM Fine Chemicals, Advanced Synthesis and Catalysis
Журнал:
Journal of the Chemical Society, Perkin Transactions 2
Дата:
2002
Аннотация:
By a chemo-enzymatic approach we performed a large-scale, stereoselective synthesis of the C<sup>α</sup>-methylated α-hydroxy acid l-(αMe)Hyv. We also prepared model depsipeptides based on this sterically demanding residue in combination with the α-amino acids l-Ala, l-Val, and Aib. From solution (FT-IR absorption and <sup>1</sup>H NMR) and crystal-state (X-ray diffraction) conformational analyses we found that l-(αMe)Hyv forces depsipeptides to fold into right-handed β-turn/helical structures by analogy with the reported propensity of l-(αMe)Val, its α-amino acid counterpart.
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