Various techniques like spectroscopy (UV-visible absorption, fluorescence, 1H-NMR), dynamic light scattering (DLS), isothermal titration calorimetry (ITC), and volumetry (density and sound velocity) have been used to throw light on the interactional behaviour of vitamin B1 i.e. thiamine hydrochloride (TH) with bovine serum albumin (BSA). The spectroscopic results revealed the preservation of tertiary structure of BSA after TH binding. The affinity value of the order of 104 M 1 has been deduced from both absorption and fluorescence titrations. Metal ion (Ca2+, Mg2+, K+, Mn2+, Na+, and Ni2+) effect on the interactional behaviour has also been monitored. The increase in the hydrodynamic size and decrease in the emission intensity through static quenching mechanism of BSA along with its non-specific nature of interactions with TH have been observed. The ionic interactions at lower TH concentrations and hydrophobic interactions at higher concentrations along with hydrational shell structural changes have been visualized from initial increase of both V and Ks values at lower while decrease at higher concentrations of TH. Calorimetric binding enthalpograms also show the initial exothermic binding process followed by endothermic. The involvement of ethylthiazolium part of TH in hydrophobic interactions whereas substituted pyrimidine ring part in hydrophilic interactions has been depicted from 1H-NMR measurements.
Compounds
#
Formula
Name
1
H2O
water
2
HK2O4P
dipotassium hydrogen phosphate
3
H2KO4P
monopotassium phosphate
Datasets
The table above is generated from the ThermoML associated json file (link above).
POMD and RXND refer to PureOrMixture and Reaction Datasets. The compound numbers are included in properties, variables, and phases, if specificied;
the numbers refer to the table of compounds on the left.