Surface recognition of a protein using designed transition metal complexes.
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.
Fazal
M A
MA
Department of Chemistry, North Dakota State University, Fargo, ND 58105, USA.
Roy
B C
BC
Sun
S
S
Mallik
S
S
Rodgers
K R
KR
D000818:Animals; D002021:Buffers; D002151:Calorimetry; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology / Q000378:metabolism; D005998:Glycine; D006639:Histidine / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D015394:Molecular Structure; D009994:Osmolar Concentration; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet
D002021:Buffers; D011506:Proteins; D006639:Histidine; D003300:Copper; D002256:Carbonic Anhydrases; D005998:Glycine