Raguse T L, Lai J R, LePlae P R, Gellman S H
Department of Chemistry, Graduate Program in Biophysics, University of Wisconsin, Madison, WI 53706, USA.
Org Lett. 2001 Nov 29;3(24):3963-6. doi: 10.1021/ol016868r.
A major frontier in foldamer research is creation of unnatural oligomers that adopt discrete tertiary structures; at present, only biopolymers are known to fold into such compact conformations. We report an initial step toward helix-bundle tertiary structure in the beta-peptide realm by showing that a 10-residue beta-peptide designed to adopt an amphiphilic helical conformation forms small soluble aggregates in water. Sedimentation equilibrium data indicate that the aggregated state falls in the tetramer-hexamer size range. [structure: see text]
折叠体研究的一个主要前沿领域是创造能呈现离散三级结构的非天然低聚物；目前，已知只有生物聚合物能折叠成这种紧密构象。我们报道了在β-肽领域迈向螺旋束三级结构的第一步，即证明一个设计成具有两亲性螺旋构象的10个残基的β-肽在水中形成小的可溶性聚集体。沉降平衡数据表明聚集态处于四聚体至六聚体的尺寸范围。[结构：见正文]
