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[Display omitted] • Date seed polyphenols were tabulated in commercial pills. • Pill's polyphenols shielded BSA versus glycoxidation via different mechanisms. • Pill's polyphenols dose-dependently inhibited formation of advanced glycation end-products. • Pill's polyphenols trapped intermediated dicarbonyls and formed some new adducts. • Pill's polyphenols declined BSA-glucose binding and structurally blocked glycoxidation sites. We aimed at tabulating and characterizing a flavan-3-ol isolated from date seeds into date seed pills (DSP) as a commercial healthcare pill, and deeply studying their anti-glycoxidation impacts on bovine serum albumin using multi-dimensional approaches SDS-PAGE/NBT, UPLC-ESI-Q-TOF-MS, antiradical via Fenton-type reaction, multispectral, and molecular docking. Results showed that DSP were successfully tabulated (an encapsulation efficiency of 98.78 %) with high antioxidant values via noncovalently binding with whey proteins supported by FTIR and lib-dock results. DSP dose-dependently decayed fluorescent-AGEs by 16.77, 5.32, and 37.41 % in DSP500-BSA-G/MGO/GO models, respectively, later confirmed by SDS-PAGE and initial precursors mitigation results. The docking results confirmed that DSP could bind with glycoxidation sites of BSA-subunits, namely Lys431, Arg458, and Arg196 via H-bonds. DSP trapped both di-carbonyls and reduced CML-level, where new adducts such as epicatechin-mono/MGO-GO, were identified. 500 µg mL−1 DSP reduced OH-induced fluorescence intensity of AGEs by 43.32 % in BSA-G/Fe2+/H 2 O 2. Our results open a new direction for upcycling by-products as effective glycoxidation inhibitors in a type of healthcare pills in protein-rich models. [ABSTRACT FROM AUTHOR]

• Mulberry anthocyanins shielded β-lactoglobulin against glycation through different mechanisms. • Mulberry anthocyanins dose-dependently mitigated creation of advanced glycation end-products. • Mulberry anthocyanins trapped glyoxal more than methylglyoxal and formed some glyoxal adducts. • Mulberry anthocyanins declined protein-glucose binding and structurally blocked lysyl sites. • Mulberry anthocyanins could be beneficially valorised as functional antiglycation ingredients. Advanced glycation end-products (AGEs), which instigate many disorders, are mostly mediated by dicarbonyl rearrangements. We studied the corresponding mechanisms of the anti-glycation effects of two anthocyanins purified from mulberry fruits, namely cyanidin 3-glucoside (C3G) and cyanidin 3-rutinoside (C3R), on glycated β-lactoglobulins (β-Lg). Both mulberry anthocyanins (MAs) inhibited the AGEs-formation in a dose-dependent manner, but the effect of C3R was significantly stronger than that of C3G (p < 0.05). MAs inhibited AGEs-formation by selectively trapping dicarbonyls, especially glyoxal. The UPLC-ESI-Q-TOF-MS results characterized that C3R formed mono- and di-glyoxal adducts, where C3G only created di-glyoxal adducts. Additionally, C3R could directly interact with some of the glycation sites of β-Lg. Overall, GO-trapping and β-Lg-MAs covalent/noncovalent binding are disclosed as the key mechanisms of the anti-AGEs activity of MAs on β-Lg, which could be valorised as effectual AGEs inhibitors in proteins-rich matrices. [ABSTRACT FROM AUTHOR]