title: Two-dimensional near-IR correlationspectroscopy study the interaction of protein and famotidine in acidic pH region.
abstract: The changing of protein in secondary structure and the binding between protein and famotidine in acid aqueous solutions were studied by Fourier-transform near-infrared spectrospy combined two-dimensional correlation analysis, pH-perturbed 2-D correlation spectra are calculated for the spectra in the 4850-4200, 7500-5350 and 6000-5000cm(-1) regions at different pH values. We observed that there is a binding between atom S of sulfanilamide radical and -COOH of protein in 5742cm(-1) and we also can explore the change of protein in the secondary structure simultaneously.
authors.affiliation: Center for Instrumental Analysis, China Pharmaceutical University, Key Laboratory of Drug Quality Control and Pharmacovigilance, Ministry of Education, Nanjing 210009, China.
authors.forename: Liyan
authors.initials: L
authors.lastname: Yu
authors.forename: Bingren
authors.initials: B
authors.lastname: Xiang
mesh_terms: D000143:Acids / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D015738:Famotidine / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013055:Spectrophotometry, Infrared / Q000379:methods*
chemical_list: D000143:Acids; D012710:Serum Albumin, Bovine; D015738:Famotidine