γ- and β‑Peptide Foldamers from Common Multifaceted Building Blocks: Synthesis and Structural Characterization

Structural characterization of 3,4-disubstituted γ-peptide and 2,3-disubstituted β-peptide foldamers derived from common multifaceted β-nitromethyl γ-amino acids and the chemical transformation of the β-nitromethyl group in γ-peptides into various functional derivatives are reported. The γ3,4-oligomers and α,γ-hybrid peptides showed characteristic C14-and C12-helical conformations in single crystals. Further, the new 2,3-disubstituted acyclic β-peptide showed the C6-helical conformation despite the poor geometry of H-bonds.

本文报道了由常见多官能β-硝甲基γ-氨基酸（β-nitromethyl γ-amino acids）衍生得到的3,4-二取代γ-肽（γ-peptide）与2,3-二取代β-肽折叠体（β-peptide foldamers）的结构表征，以及γ-肽中β-硝甲基基团向各类功能衍生物的化学转化过程。该γ3,4-寡聚体（γ3,4-oligomers）与α,γ-杂合肽（α,γ-hybrid peptides）在单晶（single crystals）中呈现特征性的C14与C12螺旋构象。此外，尽管该新型2,3-二取代无环β-肽（acyclic β-peptide）的氢键（hydrogen bonds）几何构型欠佳，但其仍展现出C6螺旋构象。