Chin. J. Org. Chem. ›› 2018, Vol. 38 ›› Issue (1): 266-271.DOI: 10.6023/cjoc201708053 Previous Articles     Next Articles

Special Issue: 庆祝吴养洁院士九十华诞专辑



赵东欣a, 吕名秀b, 马丽a, 卢奎a,b   

  1. a 河南工业大学化学化工与环境学院 郑州 450001;
    b 河南工程学院材料与化学工程学院 郑州 450007
  • 收稿日期:2017-08-24 修回日期:2017-10-11 发布日期:2017-10-16
  • 通讯作者: 赵东欣, 卢奎;
  • 基金资助:


Solid Phase Synthesis and Property of Signature Motif Ⅲ in Peptide Transporter

Zhao Dongxina, Lü Mingxiub, Ma Lia, Lu Kuia,b   

  1. a School of Chemistry, Chemical Engineering and Environment, Henan University of Technology, Zhengzhou 450001;
    b School of Material and Chemical Engineering, Henan University of Engineering, Zhengzhou 450007
  • Received:2017-08-24 Revised:2017-10-11 Published:2017-10-16
  • Contact: 10.6023/cjoc201708053;
  • Supported by:

    Project supported by the National Natural Science Foundation of China (Nos. 21572046, 21172054) and the Foundation of Scientific and Technological Project of Henan Province (No. 162102210197).

The peptide transporter family in human body is critical for the transport of peptides and drugs, and the conservative sequences in the peptide transporters play an important role in maintaining its structure and function. In order to understand the function of consensus peptides in peptide transporter and promote the application of oligopeptides in pharmaceutical and medical fields, the signature motif Ⅲ (FYLSINAGS) and its four mutants were synthesized by Fmoc solid phase synthesis method. The products were identified using mass spectrometry, and purified by RP-HPLC. The interaction between peptide and DNA was detected by UV and fluorescence spectrometry. The experimental and structural simulation results showed that the dominant role of electrostatic interaction and intercalation between oligopeptide FYLSINAGG and DNA was related to the concentration of oligopeptide FYLSINAGG, the interaction of FYGLINAGG containing helix structure and DNA was enhanced for the generation of complex, and the interaction between FYGLINKGG hasing helix structure or FYGLINSGG and DNA was attenuated. These results indicated that the serine residue in C-terminal of FYGSINAGS, and the number and position of serine in peptides had great influence on the structure of oligopeptide and its interaction with DNA. The mutation of serine into hydrophobic amino acids is beneficial to form helical structure of oligopeptides and enhance the embedded intercalation with DNA. Thus, serine residues in signature motif are important functional residues, especially at the C-terminus.

Key words: oligopeptide, solid phase synthesis, interaction, signature motif