κ-casein Inhibitors

Chemical inhibitors of κ-casein can lead to the functional disruption of this protein through various molecular interactions. Benzyl isothiocyanate can react with cysteine residues in κ-casein, forming thioureas, which may lead to structural alterations that compromise its ability to stabilize casein micelles. Similarly, Epigallocatechin gallate (EGCG) is capable of binding to κ-casein and inducing conformational changes that inhibit its micelle-stabilizing functions. Dithiothreitol (DTT) can cleave disulfide bonds within κ-casein, which are critical for maintaining its three-dimensional structure, thereby inhibiting its interaction with other casein molecules and its role in maintaining micelle structure. Chlorogenic acid and tannic acid both have the ability to non-covalently bind to hydrophobic regions or form protein complexes, respectively, which potentially alters κ-casein conformation and reduces its functional capacity in micelle stabilization.

Further, ellagic acid can bind to κ-casein and disrupt its structure, thus preventing the protein from effectively contributing to casein micelle stability. Curcumin is known to interact with κ-casein, inducing structural changes that inhibit its function in micelle formation. Genistein's protein-binding properties allow it to bind to κ-casein, potentially altering the protein's conformation and impairing its role in micelle stabilization. Caffeic acid can also bind to κ-casein, potentially altering its structural integrity and negatively impacting micelle formation. Capsaicin, with its lipophilic character, can intercalate into κ-casein's structure, disrupting necessary protein interactions for micelle stability. Quercetin and naringenin can both bind to κ-casein, leading to conformational changes that reduce the protein's effectiveness in stabilizing casein micelles. These chemical interactions with κ-casein underscore the diverse mechanisms through which the protein's functional role in micelle stability can be inhibited.