Interactions of β-Lactoglobulin With Small Molecules
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Probing the binding sites of bioactives with β-Lactoglobulin at different gastrointestinal pHs
2024, Food HydrocolloidsInteraction of β-lactoglobulin with gemcitabine based dansylated probe for its application in quantification of milk allergen
2023, Journal of Molecular LiquidsDifferentially expressed whey proteins of donkey and bovine colostrum revealed with a label-free proteomics approach
2023, Food Science and Human WellnessCitation Excerpt :Among them, β-lactoglobulin-2 (P19647) was the protein with the highest fold change value (upregulated), followed by β-lactoglobulin-1 (P13613). β-Lactoglobulin is a milk-specific protein synthesized by mammary epithelial cells and the main whey protein component in the milk of ruminants and pigs, horses, donkeys, and other animals, whereas its content in human milk is very low [41,42]. β-Lactoglobulin is a lipocalin protein that can bind many hydrophobic molecules, suggesting a role in their transport [43].
Curcumin and whey protein concentrate binding: Thermodynamic and structural approach
2023, Food HydrocolloidsRed emitting fluorogenic dye as an efficient turn-on probe for milk allergen
2022, International Journal of Biological MacromoleculesCitation Excerpt :The calyx site is cylindrical in shape having two walls of 15 Å in length and overall volume of 315 Å3. [45] In addition to these biologically important molecules, calyx site has also been found to bind various organic dye molecules via hydrophobic interaction. [16,17,45,46] Since, QR is a hydrophobic molecule; it is thus expected to bind primarily to the calyx site of β-LG protein.
An exceptionally intense turn-on fluorescence sensor in the far-red region for common milk allergen, β-lactoglobulin
2021, Sensors and Actuators, B: ChemicalCitation Excerpt :It consists of 162 amino acid residues which constitute nine β-strands labelled from A to I that form anti-parallel β-barrels with a 3-turn α-helix on the outer surface. Eight out of the nine β-strands (βA–βH) provide a cylindrical shaped central calyx, [6,41,42] (see scheme 1 ) with a dimension of ∼15 Å in length and ∼315 Å3 in volume and is responsible for the binding of various hydrophobic molecules viz, fatty acids, enzymes, vitamins and so on. [6,42] In addition to the hydrophobic binding, β-LG is also capable of binding small organic molecules via electrostatic interaction mainly with the amino acid residues present at the protein surface [42].