1414099-65-2

Upstream product

• 22529-61-9 (1R)-1-((3aR,6S,6aR)-6-(benzyloxy)-2,2-dimethyltetrahydrofuro(2,3-d)(1,3)dioxol-5-yl)ethane-1,2-diol 
• 912652-02-9 (1R)-1-[(3aR,5R,6S,6aR)-6-(benzyloxy)-2,2-dimethylperhydrofuro[2,3-d][1,3]dioxol-5-yl]-2-(tetrahydro-2H-2-pyranyloxy)ethan-1-ol 
• 1414099-34-5 C₂₁H₂₈O₇ 
• 1414099-40-3 (3aR,5R,6S,6aR)-6-(benzyloxy)-2,2-dimethyl-5-1-[(tetrahydro-2H-2-pyranyloxy)methyl]vinylperhydrofuro[2,3-d][1,3]dioxole 
• 1414099-45-8 2-[(3aR,5R,6S,6aR)-6-(benzyloxy)-2,2-dimethylperhydrofuro[2,3-d][1,3]dioxol-5-yl]-2-propen-1-ol 
• 1414099-50-5 2-[2-[(3aR,5R,6S,6aR)-6-(benzyloxy)-2,2-dimethylperhydrofuro[2,3-d][1,3]dioxol-5-yl]allyl]-1,3-isoindolinedione 
• 1414099-55-0 tert-butyl N-[2-[(3aR,5R,6S,6aR)-6-(benzyloxy)-2,2-dimethyl perhydrofuro[2,3-d]-[1,3]dioxol-5-yl]allyl]carbamate 

Relevant academic research and scientific papers

Synthesis of C-linked carbo-β2-amino acids and β2-peptides: Design of new motifs for left-handed 12/10- and 10/12-mixed helices

C-linked carbo-β2-amino acids (β2-Caa), a new class of β-amino acid with a carbohydrate side chain having d-xylo configuration, were prepared from d-glucose. The main idea behind the design of the new β-amino acids was to move the steric strain of the bulky carbohydrate side chain from the Cβ- to the Cα-carbon atom and to explore its influence on the folding propensities in peptides with alternating (R)- and (S)-β2-Caas. The tetra- and hexapeptides derived were studied employing NMR (in CDCl3), CD, and molecular dynamics simulations. The β2-peptides of the present study form left-handed 12/10- and 10/12-mixed helices independent of the order of the alternating chiral amino acids in the sequence and result in a new motif. These results differ from earlier findings on β3-peptides of the same design, containing a carbohydrate side chain with d-xylo configuration, which form exclusively right-handed 12/10-mixed helices. Quantum chemical calculations employing ab initio MO theory suggest the side chain chirality as an important factor for the observed definite left- or right-handedness of the helices in the β2- and β3-peptides.