Acta Phys. -Chim. Sin. ›› 2002, Vol. 18 ›› Issue (10): 907-910.doi: 10.3866/PKU.WHXB20021008

• ARTICLE • Previous Articles     Next Articles

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

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