title: Thermodynamic studies on the recognition of flexible peptides by transition-metal complexes.
abstract: 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.
authors.affiliation: Department of Chemistry, North Dakota State University, Fargo, North Dakota 58105, USA.
authors.forename: Shuguang
authors.initials: S
authors.lastname: Sun
authors.forename: Md Abul
authors.initials: MA
authors.lastname: Fazal
authors.forename: Bidhan C
authors.initials: BC
authors.lastname: Roy
authors.forename: Binita
authors.initials: B
authors.lastname: Chandra
authors.forename: Sanku
authors.initials: S
authors.lastname: Mallik
mesh_terms: 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
chemical_list: D010455:Peptides; D006639:Histidine; D003300:Copper