Advanced glycation end products alter the structural integrity, increase the permeability and transform the biocompatibility of collagen within the peritoneal membrane.

In patients undergoing long-term peritoneal dialysis, the peritoneal accumulation of advanced glycation end-products (AGEs) due to the Maillard reaction has long been acknowledged as problematic, although the underlying mechanisms remain insufficiently understood. Recognizing collagen as both a principal substrate for AGEs deposition and a vital cellular scaffold, we developed an innovative procedure that induces the Maillard reaction in collagen at near-physiological temperatures, enabling systematic evaluations of its structural and functional modifications. Our findings reveal that Maillard reaction-treated collagen exhibits markedly increased permeability to small- and medium-sized molecules. Furthermore, this denatured collagen diminishes the proliferative capacity of adherent mesothelial cells, implicating glycation-induced alterations in collagen in the progressive deterioration of peritoneal membrane function during extended dialysis. By illuminating previously uncharacterized morphological and functional shifts in collagen triggered by the Maillard reaction, our model provides critical insights that will enhance the safety of peritoneal dialysis and inform the development of novel therapeutic strategies.