Two-dimensional near-IR correlationspectroscopy study the interaction of protein and famotidine in acidic pH region.
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.
Yu
Liyan
L
Center for Instrumental Analysis, China Pharmaceutical University, Key Laboratory of Drug Quality Control and Pharmacovigilance, Ministry of Education, Nanjing 210009, China.
Xiang
Bingren
B
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*
D000143:Acids; D012710:Serum Albumin, Bovine; D015738:Famotidine