Biomimetic nanohydroxyapatite (nHAp) has long been used as a biocompatible material for bone repair, bone regeneration, and bone reconstruction due to its low toxicity to local or systemic tissues. Various cross-linkers have been employed to maintain the structure of collagen; these include epigallocatechin-3-gallate (EGCG), which can fortify the mechanical properties of collagen and withstand the degradation of collagenase. We hypothesized that EGCG combined with nHAp may promote resin-dentin bonding durability. Here, we examined the effect of epigallocatechin-3-gallate-encapsulated nanohydroxyapatite/mesoporous silica (EGCG@nHAp@MSN) on thermal stability and remineralization capability of dentin collagen. Dentin slices (2 × 2 × 1 mm3 ) were obtained and completely demineralized in a 10% phosphoric acid water solution. The resulting dentin collagen matrix was incubated with deionized water, EGCG, nHAp@MSN, and EGCG@nHAp@MSN. The collagen thermal degradation temperature was assessed utilizing differential scanning calorimetry analysis, which indicated that EGCG, nHAp@MSN, and EGCG@nHAp@MSN reinforced collagen's capability to resist thermal degradation. EGCG@nHAp@MSN resulted in the highest increase in denaturation temperature. Thermogravimetric analysis showed that both nHAp@MSN and EGCG@nHAp@MSN achieved a higher residual mass than the EGCG and control groups. Fourier transform infrared spectroscopy was performed to examine the interaction between EGCG@nHAp@MSN and dentin collagen. The EGCG@nHAp@MSN sample exhibited stronger dentin microhardness and uppermost bond strength after thermocycling. EGCG significantly enhanced collagen's capability to resist thermal degradation. In summary, EGCG and nHAp@MSN may work together to assist the exposed collagen to improve resistance to thermal cycling and promote remineralization while also strengthening the durability of resin-dentin bonds.
Keywords: biomodification; epigallocatechin gallate; nanohydroxyapatite/mesoporous silica; resin-dentin bonds; thermal stability.
© 2022 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.