Synthesis of a novel zwitterionic biodegradable poly (α,β-l-aspartic acid) derivative with some l-histidine side-residues and its resistance to non-specific protein adsorption

A novel zwitterionic polypeptide derivative, denoted as His-PAsp/PAsp, was successfully synthesized by amidation of Poly (α,β-l-aspartic acid) with l-histidine methyl ester. Turbidity, zeta potential and 1H NMR measurements were used to study the aggregation behaviors of His-PAsp/PAsp under different pH values. The modified polypeptide derivative composed of electro-negatively carboxylic and electro-positively imidazole residues randomly so as to bear opposite charges at pH values above or below the isoelectric point. When the zwitterionic polypeptide was coated on silicon wafer as a model substrate material, the absorption resistance of fibrinogen, a blood protein resulting in the blood coagulation cascade, on the coated surface was measured. It was found that the adsorption amount of fibrinogen on the polypeptide-coated surface depended on the dose of the polypeptide on silicon wafer. Obvious resistance of the fibrinogen adsorption on the polypeptide-coated surface was observed. Since its good biodegradability and superior anti-protein-fouling property, this pH-responsive zwitterionic polypeptide is a promising candidate for surface modification in many biomedical applications, including medical implants, drug delivery carriers, and biosensors.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► His-PAsp/PAsp zwitterionic polypeptide has been successfully synthesized by a facile way. ► The modified polypeptide derivative had an isoelectric point and bore opposite charges at pH values far high or below the isoelectric point. ► By the surface modification of zwitterionic polypeptide, the surface exhibited resistance to nonspecific protein adsorption.