物理化学学报 >> 2002, Vol. 18 >> Issue (06): 504-507.doi: 10.3866/PKU.WHXB20020606

研究论文 上一篇    下一篇

蛋白质全新设计：八残基序列形成发夹结构的圆二色谱

沙印林;黄永亮   

  1. 北京大学医学部生物物理学系,北京　100083;北京大学物理化学研究所, 北京　100871
  • 收稿日期:2001-10-30 修回日期:2001-12-17 发布日期:2002-06-15
  • 通讯作者: 沙印林 E-mail:shyl@bjmu.edu.cn

Peptide de novo Design: CD Evidences of β-hairpin Formation by Eight-residue Peptide

Sha Yin-Lin;Huang Yong-Liang   

  1. Department of Biophysics, School of Basic Medical Sciences, Peking University, Beijing　100083;Institute of Physical Chemistry, Peking University, Beijing　100871
  • Received:2001-10-30 Revised:2001-12-17 Published:2002-06-15
  • Contact: Sha Yin-Lin E-mail:shyl@bjmu.edu.cn

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摘要： β-发夹是天然蛋白质中丰富的二级结构单元之一，在蛋白折叠和功能方面扮演着重要角色.文章报导了二条多肽序列（LTVd-PGLTV，n7和 LTVGDDTV， n5）的设计、合成和园二色谱研究结果.结果显示，n5在198 nm附近呈现负峰，表现为非规整结构特征；相反，n7表现为典型的发夹结构特征，在218 nm附近呈负峰,196 nm附近呈正峰，为β-转角与β-折叠的共同贡献.初步研究表明，β-转角、序列关系和氨基酸形成β-折叠结构倾向性是β-发夹结构形成和稳定的决定性因素.

关键词: 蛋白质全新设计, β-发夹, β-转角, β-折叠, 圆二色谱, 高效液相色谱, 多肽合成

Abstract: β-hairpins are popular secondary structural elements in native protein and play important roles either in protein folds or functionalization. Here we describe the design and preliminary structural studies of two peptide sequences LTVd-PGLTV (n7) and LTVGDDTV(n5) synthesized by solid phase peptide synthetic strategy. The circular dichroism (CD)spectra of n5 show a negative minimum near 198 nm, random coil characteristics. On the contrary, the CD spectra of n7 show a minimum at about 218 nm and a maximum at about 196 nm, a typical β-hairpin characteristics, which have been concluded as the common contribution of a β-turn mixed with β-sheets. The results show that β-turn, sequence context and β-sheet forming tendency are determinant of β-hairpin formation and stability.

Key words: de novo protein design, β-hairpin, β-turn, β-sheet