Research on advanced glycation end product (AGEs) inhibition
has
generally focused on food processing, but many protein-AGEs will still
be taken. Oligopeptide (OLP)-AGEs, as the main form after digestion,
will damage human health once absorbed. Here, we investigated the
ability of lotus seedpod oligomeric procyanidins (LSOPC) to inhibit
the absorption of the OLP-AGEs and elucidated the underlying mechanism.
Our results showed that the inhibition rate of LSOPC on the absorption
of OLP-AGEs was about 50 ± 5.38%. 0.1, 0.2, and 0.3 mg/mL could
upregulate the expression of ZO-1 and downregulate the expression
of PepT1 and clathrin. Molecular docking showed that LSOPC could compete
with the binding of OLP-AGEs to PepT1 and AP-2, thus inhibiting the
absorption of OLP-AGEs. Furthermore, the interaction of LSOPC with
the OLP-AGEs reduced the surface hydrophobicity of OLP-AGEs. It altered
the secondary structure of the OLP-AGEs, thus weakening the affinity
of the OLP-AGEs to the transporter protein to inhibit the absorption
of OLP-AGEs. Together, our data revealed potential mechanisms by which
LSOPC inhibit the absorption of OLP-AGEs and opened up new perspectives
on the application of LSOPC in reducing the increasing health risks
posed by OLP-AGEs.