Progression of Self-Assembly of Amelogenin Protein Supramolecular Structures in Simulated Enamel Fluid
Engelberth, Sarah A ; Bacino, Margot S ; Sandhu, Shaiba ; Li, Wu ; Bonde, Johan LU
and Habelitz, Stefan
(2018)
In Biomacromolecules
19(10).
p.3917-3924
- Abstract
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... (More)
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.
(Less)
- author
- Engelberth, Sarah A
; Bacino, Margot S
; Sandhu, Shaiba
; Li, Wu
; Bonde, Johan
LU
and Habelitz, Stefan
- organization
- publishing date
- 2018
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biomacromolecules
- volume
- 19
- issue
- 10
- pages
- 8 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:85052308852
- pmid:30114917
- ISSN
- 1526-4602
- DOI
- 10.1021/acs.biomac.8b00808
- language
- English
- LU publication?
- yes
- id
- b031923f-c90d-4cbc-85c1-7fa7b16a31c6
- date added to LUP
- 2019-09-10 10:22:47
- date last changed
- 2024-06-27 04:39:02
@article{b031923f-c90d-4cbc-85c1-7fa7b16a31c6,
abstract = {{<p>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.</p>}},
author = {{Engelberth, Sarah A and Bacino, Margot S and Sandhu, Shaiba and Li, Wu and Bonde, Johan and Habelitz, Stefan}},
issn = {{1526-4602}},
language = {{eng}},
number = {{10}},
pages = {{3917--3924}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Biomacromolecules}},
title = {{Progression of Self-Assembly of Amelogenin Protein Supramolecular Structures in Simulated Enamel Fluid}},
url = {{http://dx.doi.org/10.1021/acs.biomac.8b00808}},
doi = {{10.1021/acs.biomac.8b00808}},
volume = {{19}},
year = {{2018}},
}