Mussel-inspired monomer – A new selective protease inhibitor against dentine collagen degradation

• Published in: Dental materials 2022-07, Vol.38 (7), p.1149-1161
• Main Authors: Li, Kang, Ngo, Fung Man, Yau, Angela Yat Laam, Tam, Winnie Wai Ling, Tse, Edmund Chun Ming, Tsoi, James Kit Hon, Yiu, Cynthia Kar Yung
• Format: Article
• Language: English
• Subjects: Cathepsin B; Cathepsins; Chlorhexidine; Collagen; Cysteine cathepsins; Dentin; Ethanol; Fluorescence; Gelatinase B; Matrix metalloproteinase; Matrix metalloproteinases; Methacrylamide; Molecular docking; Mollusks; Monomers; Mussel; Protease inhibitors; Proteinase inhibitors; Proteolysis; Variance analysis
• ISSN: 0109-5641; 1879-0097
• DOI: 10.1016/j.dental.2022.05.002

To evaluate the inhibitory effect of a novel mussel-inspired monomer (N-(3,4-dihydroxyphenethyl)methacrylamide (DMA) on the soluble and matrix-bound proteases. The inhibitory effect of DMA (0, 1, 5, and 10 mM) and 1 mM chlorhexidine (CHX) dissolved in 50% ethanol/water on soluble recombinant human matrix metalloproteinases (rhMMP-2, −8, and −9), as well as cysteine cathepsins (B and K) were evaluated using both fluorometric assay kits and molecular docking. The effect of CHX and DMA on matrix-bound proteases was examined by in situ zymography, and the fluorescence intensity and relative area were calculated by Image J software. All data obtained were analyzed by one-way ANOVA followed by Tukey test (α = 0.05). The anti-proteolytic ability of DMA increased in a dose-dependent manner except that of rhMMP-9. Inhibitory effect of 1 mM DMA against rhMMP-2, − 8, − 9, as well as cathepsin B and K was all significantly lower than 1 mM CHX (p