Surface Recognition of a Protein Using Designed Transition Metal Complexes

Abstract

Each protein has a unique pattern of histidine residues on the surface. This paper describes the design, synthesis, and binding studies of transition metal complexes to target the surface histidine pattern of carbonic anhydrase (bovine erythrocyte). When the pattern of cupric ions on a complex matches the surface pattern of histidines of the protein, strong and selective binding can be achieved in aqueous buffer (pH = 7.0). The described method of protein recognition is applicable to proteins of known structures. With rapidly increasing number of solved protein structures, the method has wide applicability in purification, targeting, and sensing of proteins.

Applications of Nanoparticles in Biology

“…[29] Another way to specifically bind proteins is through the use of transition metal complexes that can bind with surface-exposed histidines of proteins. [30] Xu et al…”

Untitled

“…Even with the potential advantages of this method, the use of DOTA to obtain DOTAMR 4 compounds has been scarcely explored. The few examples found in literature report very poor to moderate yields for DOTAM tetra-substituted compounds (11,12) and to the best of our knowledge no report for the synthesis of DOTAMR 4 amino acid or peptide derivatives when using DOTA as a starting building unit can be found. The limited use of DOTA to obtain DOTAMR 4 compounds may be attributed to its poor solubility in common organic solvents and/or the choice of the coupling agent.…”

Infinite Metal–Carboxylate Nanotube Constructed Metal–Organic Frameworks and Gas Sorption Properties

“…Synthesis of H 4 L: H 4 L was prepared according to the method published in the literature [19] (see details in the Supporting Information). Single-Crystal Structure Determination: Crystal data for H 4 L, 1, and 2 were collected with a Bruker SMART APEXII CCD diffractometer with graphite monochromated Mo-K α radiation (λ = 0.71073 Å) at room temperature.…”