Open Access(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/
Author(s) -
Cristina Peggion,
Alessandra Barazza,
Fernando Formaggio,
Marco Crisma,
Claudio Toniolo,
Marzia Villa,
Claudia Tomasini,
Herbert Mayrhofer,
Peter Pöchlauer,
Bernard Kaptein,
Quirinus B. Broxterman
Publication year - 2002
Publication title -
journal of the chemical society perkin transactions 2
Language(s) - English
Resource type - Journals
eISSN - 1472-779X
pISSN - 1364-5471
DOI - 10.1039/b107691b
Subject(s) - steric effects , chemistry , stereochemistry , residue (chemistry) , depsipeptide , enzyme , amino acid residue , stereoselectivity , organic chemistry , biochemistry , peptide sequence , catalysis , gene
By a chemo-enzymatic approach we performed a large-scale, stereoselective synthesis of the Cα-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 1H 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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