Synthetic metal-binding protein surface domains for metal ion-dependent interaction chromatography. II. Immobilization of synthetic metal-binding peptides from metal ion transport proteins as model bioactive protein surface domains.

摘要: This preliminary investigation tests the premise that biologically relevant (1) peptide-metal ion interactions, and (2) metal ion-dependent macromolecular recognition events (e.g., peptide-peptide interactions) may be modeled by biomimetic affinity chromatography. Divinylsulfone-activated agarose (6%) was used to immobilize three different synthetic peptides representing metal-binding protein surface domains from human plasma transport histidine-rich glycoprotein (HRG). The represented 1-3 multiple repeat units of 5-residue sequence (Gly-His-His-Pro-His) found in C-terminal HRG. By frontal analyses, immobilized HRG type (GHHPH)nG, where n = 1-3, were each have a similar binding capacity for both Cu(II) ions Zn(II) (31-38 mumol/ml gel). interaction variety model with peptide columns demonstrated differences selectivity despite internal homology capacity. 11-residue loaded demonstrate selective adsorption isolation proteins plasma. These results suggest selected known solvent-exposed useful systems evaluate specificity transfer vitro.