1292320-98-9

Upstream product

• 1292321-02-8 (S,S,S)-hydrochloride*NH2-γ-(Et)ACHA-OBn 
• 1292321-08-4 (S,S,S)-Boc-gabapentin-γ-OBn 
• 1292321-09-5 HCl*NH2-γ-OBn 
• 1292321-11-9 C₄₁H₆₅N₃O₆ 
• 1314654-12-0 (S,S,S,S,S,S)-Boc-gabapentin-γ-γ-OH 
• 1292320-97-8 C₅₁H₈₂N₄O₇ 
• 100-39-0 benzyl bromide 
• 1194837-06-3 (S)-2-((1S,2S)-2-nitrocyclohexyl)butan-1-ol 
• 1314654-10-8 C₁₀H₁₉NO₂ 
• 1194837-04-1 (S)-2-((1S,2S)-2-nitrocyclohexyl)butan-1-al 
• 1194837-08-5 (S)-2-((1S,2S)-2-(tert-butoxycarbonylamino)cyclohexyl)butanoic acid 
• 1194837-07-4 (S)-2-((1S,2S)-2-nitrocyclohexyl)butanoic acid: 
• 1314654-14-2 Boc-gabapentin-γ-γ-γ-OH 
• 1292321-01-7 Boc-γ-OBn 

Downstream Products

• 1314654-15-3 Boc-gabapentin-γ-γ-γ-γ-OH 
• 1292320-99-0 C₇₁H₁₁₆N₆O₉ 
• 1314654-16-4 Boc-gabapentin-γ-γ-γ-γ-γ-OH 

Relevant academic research and scientific papers

Characteristic structural parameters for the γ-peptide 14-helix: Importance of subunit preorganization

All wound up: Crystallographic data for a set of homologous peptides constructed from gabapentin and two to six preorganized γ-amino acid residues (see crystal structure of the longest peptide) allow derivation of characteristic parameters for the γ-peptide 14-helix and establish guidelines for characterizing 14-helical folding. The results suggest that the substitution pattern of a γ-residue has a profound effect on the propensity for 14-helical folding.

GAMMA AMINO ACID BUILDING BLOCKS

The invention provides compounds and methods, for example, to carry out organocatalytic Michael additions of aldehydes to cyclically constrained nitroethylene compounds catalyzed by a pro line derivative to provide cyclically constrained α-substituted-γ-n