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

Research output: Contribution to journalArticlepeer-review

22 Citations (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.

Original languageEnglish
Pages (from-to)154-158
Number of pages5
JournalFEBS Letters
Issue number1-2
Publication statusPublished - 2000 Sep 29

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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