2011
DOI: 10.1039/c1sm05018d
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In situ remineralizaiton of partially demineralized human dentine mediated by a biomimetic non-collagen peptide

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Cited by 57 publications
(63 citation statements)
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“…This specific alignment of minerals within collagen fibrils was regulated by TPP, a templating analog of NCPs . Highly negatively charged TPP accumulates within positively charged gap zones of collagen fibrils through electrostatic attraction, which further attracts fluidic PAA‐ACP nanoprecursors to enter the gap zone of collagen fibrils via electrostatic attraction . Thus, TPP functions as an ionic bridge between collagen fibrils and PAA‐ACP nanoprecursors due to the high affinity of TPP to collagen and calcium .…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…This specific alignment of minerals within collagen fibrils was regulated by TPP, a templating analog of NCPs . Highly negatively charged TPP accumulates within positively charged gap zones of collagen fibrils through electrostatic attraction, which further attracts fluidic PAA‐ACP nanoprecursors to enter the gap zone of collagen fibrils via electrostatic attraction . Thus, TPP functions as an ionic bridge between collagen fibrils and PAA‐ACP nanoprecursors due to the high affinity of TPP to collagen and calcium .…”
Section: Resultsmentioning
confidence: 99%
“…Thus, TPP functions as an ionic bridge between collagen fibrils and PAA‐ACP nanoprecursors due to the high affinity of TPP to collagen and calcium . A large fraction of the charged functional groups in the gap zone recruit and bind with calcium and phosphate ions from the PAA‐ACP nanoprecursors to precipitate electron‐dense minerals within the gap zone, which results in the observed D‐banding of collagen fibrils . In extrafibrillar mineralized collagen fibrils, D‐banding is not observed.…”
Section: Resultsmentioning
confidence: 99%
“…33,45,46 A large fraction of charged amino acid side chains in the gap zone helps to recruit and bind calcium and phosphate ions, and the resulting calcium-phosphate prenucleation cluster become crystallized HA with time. 8,34,46 Thus the gap zone of collagen fibrils serves as the entering (as inferred from the insert image in Figure 3D) and mineralization sites, which forms the D-banding of collagen fibrils (Figure 7). This is in agreement with the finding by 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 Figure 1A and Figure 2A).…”
Section: Resultsmentioning
confidence: 98%
“…Similarly, other natural or synthetic proteins 1826 and peptides 2730 (e.g. salivary proteins such as mucins, statherin, and proline rich proteins) were reported to be able to bind on the tooth surface and protect the tooth from acid attack or aid in the remineralization of the tooth 18, 31, 32 .…”
Section: Introductionmentioning
confidence: 99%
“…salivary proteins such as mucins, statherin, and proline rich proteins) were reported to be able to bind on the tooth surface and protect the tooth from acid attack or aid in the remineralization of the tooth 18, 31, 32 . While proteins or peptides can avoid the negative effect, the costs of producing these materials are high 27, 33, 34 and they may have the risk of allergic reactions for certain populations. Therefore, it is of great importance to develop an alternative non-fluoride agent which is able to effectively protect the tooth against acid erosion and/or enhance tooth remineralization safely at low cost.…”
Section: Introductionmentioning
confidence: 99%