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Grafting MAP peptide to dental polymer inhibits MMP-8 activity
Dixit, Namrata Settle, Jenifer K. Ye, Qiang Berrie, Cindy L. Spencer, Paulette Laurence, Jennifer S.
Dixit, Namrata
Settle, Jenifer K.
Ye, Qiang
Berrie, Cindy L.
Spencer, Paulette
Laurence, Jennifer S.
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Abstract
Matrix metalloproteinases (MMPs) are a class of zinc and calcium-dependent endopeptidases responsible for degrading extracellular matrix (ECM) components. Their activity is critical for both normal biological function and pathological processes (Dejonckheere et al., Cytokine Growth Factor Rev 2011;22:73–81). In dental restorations, the release and subsequent acid activation of MMPs contributes to premature failure. In particular, MMP-8 accelerates degradation by cleaving the collagen matrix within the dentin substrate in incompletely infiltrated aged bonded dentin (Buzalaf et al., Adv Dent Res 2012;24:72–76), hastening the need for replacement of restorations. Therefore, development of a dental adhesive that better resists MMP-8 activity is of significant interest. We hypothesize that modification of the polymer surface with an inhibitor would disable MMP-8 activity. Here, we identify the metal abstraction peptide (MAP) as an inhibitor of MMP-8 and demonstrate that tethering MAP to methacrylate polymers effectively inhibits catalysis. Our findings indicate complete inhibition of MMP-8 is achievable using a grafting approach. This strategy has potential to improve longevity of dental adhesives and other polymers and enable rational design of a new generation of biocompatible materials.
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Date
2015-02
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Wiley
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Keywords
MMP-8, Dental adhesive, Grafting, Inhibitor, Metal abstraction peptide, Fluorescence assay
Citation
Dixit, N., Settle, J. K., Ye, Q., Berrie, C. L., Spencer, P., & Laurence, J. S. (2015). Grafting MAP peptide to dental polymer inhibits MMP-8 activity. Journal of Biomedical Materials Research. Part B, Applied Biomaterials, 103(2), 324–331. http://doi.org/10.1002/jbm.b.33205