Next Article in Journal
Sex-Specific SARS-CoV-2 Mortality: Among Hormone-Modulated ACE2 Expression, Risk of Venous Thromboembolism and Hypovitaminosis D
Next Article in Special Issue
Signal Deconvolution and Noise Factor Analysis Based on a Combination of Time–Frequency Analysis and Probabilistic Sparse Matrix Factorization
Previous Article in Journal
Aedes albopictus Autophagy-Related Gene 8 (AaAtg8) Is Required to Confer Anti-Bacterial Gut Immunity
Previous Article in Special Issue
Dynamics Studies of DNA with Non-canonical Structure Using NMR Spectroscopy
Open AccessArticle

Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin

by Jing Zhang 1,2,3, Jian Wang 1, Chengwei Ma 1 and Junxia Lu 1,*
1
School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China
2
State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China
3
University of Chinese Academy of Sciences, Beijing 100049, China
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(8), 2946; https://doi.org/10.3390/ijms21082946
Received: 18 February 2020 / Revised: 28 March 2020 / Accepted: 7 April 2020 / Published: 22 April 2020
Tooth enamel is formed in an extracellular environment. Amelogenin, the major component in the protein matrix of tooth enamel during the developing stage, could assemble into high molecular weight structures, regulating enamel formation. However, the molecular structure of amelogenin protein assembly at the functional state is still elusive. In this work, we found that amelogenin is able to induce calcium phosphate minerals into hydroxyapatite (HAP) structure in vitro at pH 6.0. Assessed using X-ray diffraction (XRD) and 31P solid-state NMR (SSNMR) evidence, the formed HAP mimics natural enamel closely. The structure of amelogenin protein assembly coexisting with the HAP was also studied using atomic force microscopy (AFM), transmission electron microscopy (TEM) and XRD, indicating the β-amyloid structure of the protein. SSNMR was proven to be an important tool in detecting both the rigid and dynamic components of the protein assembly in the sample, and the core sequence 18EVLTPLKWYQSI29 was identified as the major segment contributing to the β-sheet secondary structure. Our research suggests an amyloid structure may be an important factor in controlling HAP formation at the right pH conditions with the help of other structural components in the protein assembly. View Full-Text
Keywords: amelogenin; hydroxyapatite; enamel biomimetic; protein assembly structure; solid-state NMR amelogenin; hydroxyapatite; enamel biomimetic; protein assembly structure; solid-state NMR
Show Figures

Figure 1

MDPI and ACS Style

Zhang, J.; Wang, J.; Ma, C.; Lu, J. Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin. Int. J. Mol. Sci. 2020, 21, 2946.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop