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Casein–whey protein–protein interfaces refer to the biochemical and structural contact zones formed between the two major protein fractions in bovine milk: the casein micelles and the globular whey proteins. These interfaces are primarily established during industrial processing, such as heat treatment, which triggers the denaturation of whey proteins (notably beta-lactoglobulin) and their subsequent conjugation to kappa-casein via thiol-disulfide exchange (Singh, 2004, International Dairy Journal). While these interactions are of paramount importance in food rheology and dairy technology for controlling product texture and stability, they do not serve as therapeutic targets for drug intervention in human physiology (Donato & Guyomarc'h, 2009, Dairy Science & Technology). In the context of human health, these interfaces are studied for their impact on the gastrointestinal digestion of milk and their role in modulating the allergenicity of dairy products (Villa et al., 2018, Nutrients). The formation of these complexes can either mask or expose specific epitopes, thereby influencing the recognition of milk proteins by IgE antibodies in allergic individuals. Consequently, this 'target' is a structural feature of food chemistry rather than a biological receptor or enzyme involved in disease pathogenesis. Research into these interfaces often utilizes advanced imaging and spectroscopic techniques to map the spatial distribution of proteins within the dairy matrix. Understanding the stability of these interfaces is crucial for the development of specialized infant formulas and clinical nutrition products.
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