物理化学学报 >> 2002, Vol. 18 >> Issue (10): 907-910.doi: 10.3866/PKU.WHXB20021008

研究论文 上一篇    下一篇

β-发夹多肽的全新设计和构象研究

沙印林;李银玲;邱阳;王琦;来鲁华;唐有祺   

  1. 北京大学基础医学院生物物理学系，单分子与纳米生物医学实验室，北京　100083;北京大学物理化学研究所, 北京　100871
  • 收稿日期:2002-02-25 修回日期:2002-04-08 发布日期:2002-10-15
  • 通讯作者: 沙印林 E-mail:shyl@bjmu.edu.cn

de novo Design and Conformational Studies of a β-hairpin Forming Peptide

Sha Yin-Lin;Li Yin-Ling;Qiu Yang;Wang Qi;Lai Lu-Hua;Tang You-Qi   

  1. Single Molecule and Nano-biomedicine Laboratory, Department of Biophysics, School of Basic Medical Sciences, Peking University, Beijing　100083;Institute of Physical Chemistry, Peking University, Beijing　100871
  • Received:2002-02-25 Revised:2002-04-08 Published:2002-10-15
  • Contact: Sha Yin-Lin E-mail:shyl@bjmu.edu.cn

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摘要： 引入跨股氨基酸队的方法进行β-发夹结构的设计，序列[R1G2T3F4W5V6d-P7S8V9N10Y11F12, β2] 中包含二个氨基酸对V6V9和F4Y11，并以d-P7S8作转角来稳定结构.多肽合成采用Fmoc/But固相合成方法.圆二色谱研究显示，β2在202 nm呈现正峰，在217.5 nm处呈负峰，为β转角和β折叠共同贡献的叠加，是典型的β-发夹结构圆二色谱特征.红外光谱研究进一步验证了圆二色谱的结果，表明β2在溶液中主要以β-发夹结构存在.

关键词: 全新设计, β-发夹, β-转角, β-折叠片, 跨股氨基酸对, 　圆二色谱, 红外光谱

Abstract: A 12-residue peptide (R1G2T3F4W5V6d-P7S8V9N10Y11F12, β2) with cross-strand amino acid pairs V6V9, F4Y11 and Y3F12, predicted to form β-hairpin, was designed and synthesized by Fmoc/But strategy. The circular dichroism spectrum ofβ2 in PBS buffer shows a maximum at about 202 nm and a minimum at about 217.5 nm, a typical β-hairpin characteristics that have been postulated as the common contribution from a β-turn mixed with a β-sheet. The FT-IR experiments confirmed the secondary structural contents of β2.

Key words: de novo design, β-hairpin, β-turn, β-sheet, Cross-strand amino acid pairs, CD, FT-IR