Resveratrol Effect on α-Lactalbumin Thermal Stability.

ABSTRACT: The effect of resveratrol (RESV) on α-lactalbumin (α-LA) thermal stability was evaluated using differential scanning calorimetry (DSC), circular dichroism (CD) and dynamic light scattering (DLS) measurements. Complementary information offered by molecular docking served to identify the binding site of the ligand on the native structure of protein and the type of interacting forces. DSC thermograms revealed a double-endotherm pattern with partial overlapping of the two components. The most relevant effect of RESV is manifested in the narrowing of the protein thermal fingerprint: the first process (peak temperature T₁) is shifted to higher temperatures while the second one (peak temperature T₂) to lower values. The CD data indicated partial conformational

SUBMITTER: Precupas A 

PROVIDER: S-EPMC11504486 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature