NONSPECIFIC-BINDING OF LYSINE-GLUCOSE-DERIVED MAILLARD PRODUCTS TO MACROPHAGES OUTWEIGHS SPECIFIC RECEPTOR-MEDIATED INTERACTIONS

Studies on the binding of lysine-glucose-derived Maillard products to siliconised assay tubes indicate that caution must be exercised when i nterpreting binding parameters, owing to the saturable binding kinetic s observed (B-max = 490 pmol, K-d = 22.2/nM). When these are taken int o account, kinetic studies on the binding of such late-stage Maillard products to macrophages show that any specific receptor binding is swa mped by non-specific binding to both cell lines and native macrophages , as neither binding saturation nor cross-competition (homologous or h eterologous) was detected. This has implications for the role of macro phages in the recognition of Maillard products, and suggests that non- specific binding may be quantitatively more important than specific re ceptor binding in the cellular recognition of such food products.