Thermodynamic studies on the recognition of flexible peptides by transition-metal complexes.
Strong and selective binding to a trihistidine peptide has been achieved employing Cu(2+)-histidine interactions in aqueous medium (25 mM HEPES buffer, pH 7.0). When the pattern of cupric ions on a complex matched with the pattern of histidines on the peptide, a strong and selective binding was observed. UV-vis spectroscopic studies show that the cupric ions coordinate to the histidines of the peptides. Thermodynamic studies reveal that the binding process is enthalpy driven over the entire range of working temperature (25-40 degrees C). An enthalpy-entropy compensation effect was also observed.
Sun
Shuguang
S
Department of Chemistry, North Dakota State University, Fargo, North Dakota 58105, USA.
Fazal
Md Abul
MA
Roy
Bidhan C
BC
Chandra
Binita
B
Mallik
Sanku
S
D001665:Binding Sites; D002151:Calorimetry; D002384:Catalysis; D003300:Copper / Q000737:chemistry; D006639:Histidine / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
D010455:Peptides; D006639:Histidine; D003300:Copper