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Synthesis, characterization, and conformational analysis by FT-IR absorption, 1 H NMR and X-ray diffraction techniques are described for a series of side-chain O-glycosylated Thr peptides of different main-chain length rich in the helicogenic Aib residue. The results obtained, compared with those of related peptides containing side-chain protected Thr and Ser residues and host Aib homo-oligomers,...
The crystal structure of the fully protected glycotripeptide N-benzyloxycarbonyl-O-(2,3,4,6-tetra-O-acetyl-β-d-galactopyranosyl)-l-threo nyl-α-aminoisobutyryl-α-aminoisobutyric acid tert-butyl ester [Z-(β-d-GalAc 4 )-l-Thr-Aib-Aib-OtBu] has been determined by X-ray diffraction. The peptide backbone is fully extended at Thr(1), left-handed helical at Aib(2), while it is right-handed helical...
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