Synthetic Protein Surface Domains as Bioactive Stationary Phases

摘要: Significant developments toward the site- or domain-specific interaction of proteins with chemically defined stationary phases have been made during last 10 to 20 years. Most these efforts, however, were focused primarily on need for improved protein purification strategies. One example was introduction new chemical methods immobilization transition-metal ions (Porath et al., 1975; Porath and Olin, 1983). Immobilized metal ion affinity chromatography (IMAC), although relatively slow gain widespread acceptance, is clearly an important advancement in field purification. In our view, use immobilized can address questions that go beyond Indeed, interactions peptides surface-immobilized presents opportunity investigate ultimately model biospecific ion-dependent macromolecular recognition events. To help explore development this opportunity, we evaluated (1) surface—metal mechanisms (Hutchens 1988, 1989b; Hutchens Li, 1988; Yip, 1990a,b, 1992a,b; Yip 1989; Hutchens, 1989), (2) surface 1981, 1989b), (3) evaluate ligand-induced alterations macro-molecular structure 1990; 1991b). We shown both qualitative quantitative examples variability selectivity biomolecular ions. Until recently, efforts area limited simple, (i. e., nonbiological) stationary-phase chelators type introduced by co-workers