title: Multi-spectroscopic and voltammetric evidences for binding, conformational changes of bovine serum albumin with thiamine.
abstract: The interaction between thiamine hydrochloride (TA) and bovine serum albumin (BSA) was investigated by fluorescence, FTIR, UV-vis spectroscopic and cyclic voltammetric techniques under optimised physiological condition. The fluorescence intensity of BSA is gradually decreased upon addition of TA due to the formation of a BSA-TA complex. The binding parameters were evaluated and their behaviour at different temperatures was analysed. The quenching constants (Ksv) obtained were 2.6 × 104, 2.2 × 104and 2.0 × 104L mol-1at 288, 298 and 308 K, respectively. The binding mechanism was static-type quenching. The values of ΔH° and ΔS° were found to be 26.87 kJ mol-1and 21.3 J K-1mol-1, and indicated that electrostatic interaction was the principal intermolecular force. The changes in the secondary structure of BSA upon interaction with TA were confirmed by synchronous and 3-D spectral results. Site probe studies reveal that TA is located in site I of BSA. The effects of some common metal ions on binding of BSA-TA complex were also investigated.
authors.affiliation: a P. G. Department of Studies in Chemistry , Karnatak University , Dharwad , India.
authors.forename: Atmanand M
authors.initials: AM
authors.lastname: Bagoji
authors.affiliation: b Department of Chemistry , P. C. Jabin Science College , Hubli , India.
authors.forename: Jayant I
authors.initials: JI
authors.lastname: Gowda
authors.affiliation: a P. G. Department of Studies in Chemistry , Karnatak University , Dharwad , India.
authors.forename: Naveen M
authors.initials: NM
authors.lastname: Gokavi
authors.affiliation: a P. G. Department of Studies in Chemistry , Karnatak University , Dharwad , India.
authors.forename: Sharanappa T
authors.initials: ST
authors.lastname: Nandibewoor
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D055664:Electrochemical Techniques / Q000379:methods*; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry / Q000379:methods*; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared; D055672:Static Electricity; D013816:Thermodynamics; D013831:Thiamine / Q000737:chemistry / Q000378:metabolism*
chemical_list: D008670:Metals; D012710:Serum Albumin, Bovine; D013831:Thiamine
keywords: binding; bovine serum albumin; cyclic voltammetry; fluorescence; quenching; thiamine hydrochloride