New Perspective on the Interaction Behavior Between Riboflavin and β Lactoglobulin-β Casein Complex by Biophysical Techniques

Dynamic Observation of the Membrane Interaction Processes of β-Lactoglobulin by Time-Resolved Vacuum-Ultraviolet Circular Dichroism

“…Bovine β-lactoglobulin (bLG) is one of the major proteins found in milk and many other mammals. A considerable body of research has revealed the structures and functions of bLG, demonstrating that this protein has a hydrophobic binding site inside the β-barrel structure against numerous amphiphilic or hydrophobic compounds such as antioxidant and anti-inflammatory substrates, indicating the possibility of functioning as a material transporter. − Furthermore, the β-strand-rich structure of bLG is altered to produce an α-helix-rich structure, similar to its molten globule structure after treatment with not only surfactants such as N -alkyl sulfate and sodium dodecyl sulfate ,, but also micelle and liposome membranes composed of lipid molecules, suggesting the functionality of bLG as an intercellular transporter . Several studies have also suggested that helical alternation or membrane interaction increases at low pH and without salt because both conditions enhance the electrostatic interaction between the positively charged regions of bLG and the negatively charged liposome surface. , Furthermore, it was found that the micelle membrane promoted helix formation or strength of interaction because the larger curvature or looser packing density of the micelle surface, compared to those of the liposome ones, allowed the bLG hydrophobic region to easily access the inside of the membrane .…”