The interaction between vitamin B2 (VB2), a type of necessary nutrient for the body’s metabolism and repair, and trypsin, a serine protease found in the digestive system, has been investigated in vitro under a simulated physiological condition by UV–Vis spectrophotometry and fluorescence spectrometry. The intrinsic fluorescence intensity of trypsin was strongly quenched by VB2. Spectrophotometric observations are rationalized in terms of a static quenching process at lower concentrations of VB2 and a combined quenching (both dynamic and static) process at higher concentrations of VB2. The binding parameters, such as the binding constants and the number of binding sites, can be evaluated by fluorescence quenching experiments. The apparent binding constants K between VB2 and trypsin at different temperatures were 1.406, 1.264, and 0.543 × 106 L mol−1 and the numbers of binding sites n were 1.386, 1.391, and 1.319, which were all evaluated by the fluoresence quenching experiments. The negative values of ΔG for the formation of the trypsin–VB2 complex implied that the binding was a spontaneous process. According to the van’t Hoff equation, the standard enthalpy change (ΔH) and standard entropy change (ΔS) for the reaction were calculated to be −49.817 kJ mol−1 and −56.219 J mol−1 K−1, respectively, indicating that the hydrophobic interaction played a significant role in VB2 binding to trypsin. In addition, the binding distance between VB2 (acceptor) and trypsin (donor) was estimated to be 1.11 nm according to Förster’s resonance energy transfer theory. The results obtained here will be of biological significance in pharmacology and clinical medicine.
Research on Chemical Intermediates – Springer Journals
Published: Mar 29, 2013
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