Progression of Self-Assembly of Amelogenin Protein Supramolecular Structures in Simulated Enamel Fluid.
Progression of Self-Assembly of Amelogenin Protein Supramolecular Structures in Simulated Enamel Fluid.
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DOI:
10.1021/acs.biomac.8b00808
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发表时间:
2018-10-08
影响因子:
6.2
通讯作者:
Habelitz S
中科院分区:
文献类型:
--
作者:
Engelberth SA;Bacino MS;Sandhu S;Li W;Bonde J;Habelitz S
Mechanisms of protein-guided mineralization in enamel, leading to organized fibrillar apatite nanocrystals, remain elusive. In vitro studies reveal recombinant human amelogenin (rH174), a matrix protein templating this process, self-assembles into a variety of structures. This study endeavors to clarify the self-assembly of rH174 in physiologically relevant conditions. Self-assembly in simulated enamel fluid was monitored up to 2 months. At alkali (7.3–8.7) and acidic (5.5–6.1) pH ranges, a distinct progression in formation was observed from nanospheres (17–23 nm) to intermediate-length nanorods, concluding with the formation of long 17–18 nm wide nanoribbons decorated with nanospheres. Assembly in acidic condition progressed quicker to nanoribbons with fewer persistent nanospheres. X-ray diffraction exhibited reflections characteristic of antiparallel β-sheets (4.7 and 9.65 Å), supporting the model of amyloid-like nanoribbon formation. This is the first observation of rH174 nanoribbons at alkaline pH as well as concurrent nanosphere formation, indicating both supramolecular structures are stable together under physiological conditions.
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DOI:
10.1155/2013/684607
发表时间:
2013-09-16
期刊:
ISRN dentistry
影响因子:
--
作者:
Bartlett JD
通讯作者:
Bartlett JD
影响因子:
4.6
作者:
Carneiro KM;Zhai H;Zhu L;Horst JA;Sitlin M;Nguyen M;Wagner M;Simpliciano C;Milder M;Chen CL;Ashby P;Bonde J;Li W;Habelitz S
通讯作者:
Habelitz S
影响因子:
3.6
作者:
DIEKWISCH, TGH;BERMAN, BJ;SLAVKIN, HC
通讯作者:
SLAVKIN, HC
影响因子:
4.8
作者:
Bromley, Keith M.;Kiss, Andrew S.;Moradian-Oldak, Janet
通讯作者:
Moradian-Oldak, Janet
影响因子:
3
作者:
FINCHAM, AG;MORADIANOLDAK, J;SLAVKIN, HC
通讯作者:
SLAVKIN, HC