Please use this identifier to cite or link to this item:
https://doi.org/10.1021/cg300754a
DC Field | Value | |
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dc.title | Amelogenin processing by MMP-20 prevents protein occlusion inside calcite crystals | |
dc.contributor.author | Bromley, K.M. | |
dc.contributor.author | Lakshminarayanan, R. | |
dc.contributor.author | Thompson, M. | |
dc.contributor.author | Lokappa, S.B. | |
dc.contributor.author | Gallon, V.A. | |
dc.contributor.author | Cho, K.R. | |
dc.contributor.author | Qiu, S.R. | |
dc.contributor.author | Moradian-Oldak, J. | |
dc.date.accessioned | 2014-06-23T05:31:41Z | |
dc.date.available | 2014-06-23T05:31:41Z | |
dc.date.issued | 2012-10-03 | |
dc.identifier.citation | Bromley, K.M., Lakshminarayanan, R., Thompson, M., Lokappa, S.B., Gallon, V.A., Cho, K.R., Qiu, S.R., Moradian-Oldak, J. (2012-10-03). Amelogenin processing by MMP-20 prevents protein occlusion inside calcite crystals. Crystal Growth and Design 12 (10) : 4897-4905. ScholarBank@NUS Repository. https://doi.org/10.1021/cg300754a | |
dc.identifier.issn | 15287483 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/75547 | |
dc.description.abstract | Calcite crystals were grown in the presence of full-length amelogenin and during its proteolysis by recombinant human matrix metalloproteinase 20 (rhMMP-20). Recombinant porcine amelogenin (rP172) altered the shape of calcite crystals by inhibiting the growth of steps on the {104} faces and became occluded inside the crystals. Upon co-addition of rhMMP-20, the majority of the protein was digested resulting in a truncated amelogenin lacking the C-terminal segment. In rP172-rhMMP-20 samples, the occlusion of amelogenin into the calcite crystals was drastically decreased. Truncated amelogenin (rP147) and the 25-residue C-terminal domain produced crystals with regular shape and less occluded organic material. Removal of the C-terminal diminished the affinity of amelogenin to the crystals and therefore prevented occlusion. We hypothesize that hydroxyapatite (HAP) and calcite interact with amelogenin in a similar manner. In the case of each material, full-length amelogenin binds most strongly, truncated amelogenin binds weakly, and the C-terminus alone has the weakest interaction. Regarding enamel crystal growth, the prevention of occlusion into maturing enamel crystals might be a major benefit resulting from the selective cleavage of amelogenin at the C-terminus by MMP-20. Our data have important implications for understanding the hypomineralized enamel phenotype in cases of amelogenesis imperfecta resulting from MMP-20 mutations and will contribute to the design of enamel inspired biomaterials. © 2012 American Chemical Society. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/cg300754a | |
dc.source | Scopus | |
dc.type | Article | |
dc.contributor.department | CHEMISTRY | |
dc.description.doi | 10.1021/cg300754a | |
dc.description.sourcetitle | Crystal Growth and Design | |
dc.description.volume | 12 | |
dc.description.issue | 10 | |
dc.description.page | 4897-4905 | |
dc.description.coden | CGDEF | |
dc.identifier.isiut | 000309493300030 | |
Appears in Collections: | Staff Publications |
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