Add time:07/16/2019         Source:sciencedirect.com

The study describes the synthesis of new β2,2-peptides made from geminally disubstituted β2,2-amino acid and their folding propensities. The (R)-C-linked carbo-β2,2-amino acid [(R)-β2,2-Caa] was prepared from d-glucose and converted into the homo-oligomeric di-, tetra-, and hexapeptides. The conformational studies were carried out using NMR (in CDCl3), CD, IR, and MD calculations. These β2,2-peptides were interestingly stabilized by five-membered (mr) inter-residue H-bonds NH(i)⋯O(i-1) (furanoside) and a 6-mr intra-residue H-bond between amide proton (NH(i)) and the oxygen of –OMe(i) at the C3 carbon of the carbohydrate side chain. These results amply demonstrate that the ‘epimerization’ at the spiro carbon center has an effect on the conformational behavior of these peptides. Finding of these, H-bonding patterns, which are not so common to stabilize the folds in this class of β2,2-Caa derived peptides would further facilitate augmentation in the domain of foldamer.

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