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.
(αMe)Hyv: Chemo-enzymatic synthesis, and preparation and preferred conformation of model depsipeptides / Peggion C.; Barazza A.; Formaggio F.; Crisma M.; Toniolo C.; Villa M.; Tomasini C.; Mayrhofer H.; Pochlauer P.; Kaptein B.; Broxterman Q.B.. - In: JOURNAL OF THE CHEMICAL SOCIETY. PERKIN TRANSACTIONS 2. - ISSN 1364-5471. - STAMPA. - -:3(2002), pp. 644-651.
(αMe)Hyv: Chemo-enzymatic synthesis, and preparation and preferred conformation of model depsipeptides
Tomasini C.Conceptualization
;
2002
Abstract
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
