AI Article Synopsis
- The study focused on the binding interactions between bovine serum albumin (BSA) and curcumin, revealing a 1:1 binding ratio but varying thermodynamic properties depending on the experimental technique used.
- Different methods yielded different binding constants, showing that BSA can influence curcumin stability in terms of photodegradation.
- Results highlighted the importance of using multiple techniques to fully understand protein-ligand interactions, as thermodynamic parameters differed significantly between native and unfolded forms of BSA.
Article Abstract
Bovine serum albumin (BSA)/curcumin binding and dye photodegradation stability were evaluated. BSA/curcumin complex showed 1:1 stoichiometry, but the thermodynamic binding parameters depended on the technique used and BSA conformation. The binding constant was of the order of 10L·mol by fluorescence and microcalorimetric, and 10 and 10L·mol by surface plasmon resonance (steady-state equilibrium and kinetic experiments, respectively). For native BSA/curcumin, fluorescence indicated an enthalpic and entropic driven process based on the standard enthalpy change (ΔH=-8.67kJ·mol), while microcalorimetry showed an entropic driven binding process (ΔH=29.11kJ·mol). For the unfolded BSA/curcumin complex, it was found thatp ΔH=-16.12kJ·mol and ΔH=-42.63kJ·mol. BSA (mainly native) increased the curcumin photodegradation stability. This work proved the importance of using different techniques to characterize the protein-ligand binding.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.foodchem.2017.09.092 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!