Binding of a de novo designed peptide to specific glycosaminoglycans

FEBS Letters

Chien, K.Y¹  Fang, J.C¹  Liu, Y.J¹  Jayaraman, G¹  Lyu, P.C¹  Wu, C.W¹ 

[1] Department of Life Sciences, National Tsing Hua University, Hsinchu 30043, Taiwan

关键词: De novo design;    Lysine rich peptide;    Glycosaminoglycan;    Induced helix;    Binding specificity;    Electrostatic interaction;   

DOI  :  10.1016/S0014-5793(00)01964-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown