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The durability of resin–dentine bonds are enhanced by epigallocatechin‐3‐gallate‐encapsulated nanohydroxyapatite/mesoporous silica

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 epigallo...

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Detalles Bibliográficos
Autores principales: Zhang, Taiyang, Deng, Wei, Zhang, Ying, Liu, Ming, Ling, Yongchang, Sun, Qiurong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9811609/
https://www.ncbi.nlm.nih.gov/pubmed/36350226
http://dx.doi.org/10.1002/2211-5463.13521
Descripción
Sumario: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 mm(3)) 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.