Binding of a de novo designed peptide to specific glycosaminoglycans

G. Jayaraman, C. W. Wu, Y. J. Liu, K. Y. Chien, J. C. Fang, P. C. Lyu

研究成果: Article同行評審

22 引文 斯高帕斯(Scopus)


The binding of glycosaminoglycans to a synthetic peptide (SKAQKAQAKQAKQAQKAQKAQAKQAKQW-CONH2), consisting of a hybrid consensus heparin binding sequence, is studied using circular dichroism, fluorescence anisotropy and nuclear magnetic resonance techniques. The results unveil certain novel features, most importantly, the peptide binds preferentially to iduronic acid containing glycosaminoglycans and the dissociation constant for the peptide-heparin complex was found to be 30 nM. Interestingly, higher order intermolecular association(s)/aggregation was not observed, especially at saturating concentrations of the ligand. The helical structure of the peptide backbone, induced upon binding to a particular glycosaminoglycan is directly related to their binding affinity. In our opinion, studies on such unconventional hybrid peptide sequences containing low density basic amino acid residues would lead to the design of sequence specific glycosaminoglycan binding peptides. Copyright (C) 2000 Federation of European Biochemical Societies.

頁(從 - 到)154-158
期刊FEBS Letters
出版狀態Published - 2000 九月 29

All Science Journal Classification (ASJC) codes

  • 生物物理學
  • 結構生物學
  • 生物化學
  • 分子生物學
  • 遺傳學
  • 細胞生物學


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