The roles of 10-methacryloyloxydecyl dihydrogen phosphate and its calcium salt in preserving the adhesive–dentin hybrid layer.

10-Methacryloyloxydecyl dihydrogen phosphate (MDP) has been regarded as the most effective dentin-bonding monomer for more than 20 years. Although the dentin-bonding promoting effect of MDP has been well demonstrated, the mechanisms by which it benefits the stably of collagen within the adhesive–dentin hybrid layer are not currently fully understood. The objective of this study was to investigate the roles of MDP and its calcium salt in preserving the adhesive–dentin hybrid layer. MDP-conditioned collagen was investigated by Fourier-transform infrared spectroscopy, Ultraviolet–visible spectroscopy, and molecular docking. The structural changes to the dentin surface upon acid-etching and MDP-conditioning were observed by SEM. X-ray diffraction and nuclear magnetic resonance were used to investigate the chemical interactions between MDP and HAp. The collagen-protecting effects of MDP and its Ca salt were investigated using in-situ zymography, rhMMP-9 colorimetric assay, hydroxyproline assay, and molecular docking. MDP forms a stable collagen-phosphate complex through hydrogen bonding with the collagen in dentin. Furthermore, it generates MDP-Ca salts that are deposited on the dentin collagen scaffold, protecting it from degradation. Moreover, both free MDP and the MDP-Ca salt inhibit matrix metallopeptidase and exogenous proteases, with the inhibitory effect of the calcium salt being significantly stronger than that of the free form. MDP-based adhesives preserve the collagen within the hybrid layer by simultaneously improving collagen's resistance to exogenous enzymes and inhibiting MMP activity, both of which contribute to the longevity of dentin–resin bonding. [Display omitted] • MDP-Ca salt is deposited on the dentin collagen scaffold to protect the collagen. • Both free MDP and the formed MDP-Ca salt inhibit MMP-9 directly. • MDP and MDP-Ca salt improve collagen resistance against exogenous proteases. • MDP exhibits a hydrophobic effect and stable binding to type-I collagen. [ABSTRACT FROM AUTHOR]