The interaction and binding of flavonoids to human serum albumin modify its conformation, stability and resistance against aggregation and oxidative injuries

• Published in: Biochimica et biophysica acta. General subjects Vol. 1861; no. 1; pp. 3531 - 3539
• Main Authors: Barreca, Davide, Laganà, Giuseppina, Toscano, Giovanni, Calandra, Pietro, Kiselev, Mikhail A., Lombardo, Domenico, Bellocco, Ersilia
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.01.2017
• Subjects: Binding Sites; electrophoresis; Flavonoid; flavonoids; Flavonoids - metabolism; Fluorescence; Fourier transform infrared spectroscopy; FTIR; glucose; Human serum albumin; Humans; hydrogen bonding; hydrophobicity; ligands; medicinal properties; Microscopy, Fluorescence; Models, Molecular; molecular models; oxidation; Oxidative Stress; Oxidative stresses and protein fibrillation; Phloretin - chemistry; Protein Aggregates; Protein Binding; Protein Conformation; protein degradation; protein structure; Proteolysis; Serum Albumin - chemistry; Serum Albumin - metabolism; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Thermodynamic and kinetic variations; Thermodynamics; Fluorescence; Human serum albumin; Thermodynamic and kinetic variations; Flavonoid; FTIR; Oxidative stresses and protein fibrillation

Interactions of ligands with proteins imply changes in the properties of the macromolecules that may deeply modify their biological activities and conformations and allow them to acquire new and, sometimes, unexpected abilities. The flavonoid phloretin has several pharmacological properties that are...