Zhang Yanfeng, Lu Hua, Lin Yao, Cheng Jianjun
Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Macromolecules. 2011 Sep 13;44(17):6641-6644. doi: 10.1021/ma201678r.
Water-soluble polypeptides adopting α-helical conformations with unprecedented high helicities were obtained by elongating the charge-containing side chains of the constituent amino acids to allow the terminal charges to be situated distally from the peptide backbone. Poly(γ-(4-aminoethylthiopropoxyl)-benzyl-(L)-glutamate) (PAOBLG-AET) with a charge-peptide backbone distance of 17 σ-bonds exhibited a remarkably high helical content (81%) at a degree of polymerization as low as 10. The helical conformations of these short polypeptides were very stable against various harsh, protein-denaturing conditions, such as extreme pH, high temperature, and high salt or urea concentrations.
通过延长组成氨基酸的含电荷侧链，使末端电荷远离肽主链，获得了具有前所未有的高螺旋度的α-螺旋构象的水溶性多肽。电荷-肽主链距离为17个σ键的聚（γ-（4-氨基乙基硫代丙氧基）-苄基-（L）-谷氨酸）（PAOBLG-AET）在低至10的聚合度下表现出非常高的螺旋含量（81%）。这些短多肽的螺旋构象在各种苛刻的、使蛋白质变性的条件下非常稳定，如极端pH值、高温以及高盐或尿素浓度。
