Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin
2020-04
Source PublicationINTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
EISSN1422-0067
Volume21Issue:8
Status已发表
DOI10.3390/ijms21082946
AbstractTooth 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 P-31 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 beta-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 (18)EVLTPLKWYQSI(29) was identified as the major segment contributing to the beta-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.
Keywordamelogenin hydroxyapatite enamel biomimetic protein assembly structure solid-state NMR
URL查看原文
Indexed BySCI ; SCIE
Language英语
Funding ProjectNational Science Foundation of China[31770790] ; Yangfan program of Shanghai municipal government[19YF1433500]
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS SubjectBiochemistry & Molecular Biology ; Chemistry, Multidisciplinary
WOS IDWOS:000535565300288
PublisherMDPI
WOS KeywordSOLID-STATE NMR ; CALCIUM PHOSPHATES ; ENAMEL ; ASSIGNMENT ; BACKBONE ; SPECTROSCOPY ; IMPERFECTA ; PROTEINS
Original Document TypeArticle
Citation statistics
Document Type期刊论文
Identifierhttps://kms.shanghaitech.edu.cn/handle/2MSLDSTB/121626
Collection生命科学与技术学院_硕士生
生命科学与技术学院_PI研究组_陆珺霞组
生命科学与技术学院_公共科研平台_分子细胞学平台
生命科学与技术学院_博士生
Corresponding AuthorLu, Junxia
Affiliation
1.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China
2.Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, CAS Ctr Excellence Mol Cell Sci, State Key Lab Mol Biol, Shanghai 200031, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
First Author AffilicationSchool of Life Science and Technology
Corresponding Author AffilicationSchool of Life Science and Technology
First Signature AffilicationSchool of Life Science and Technology
Recommended Citation
GB/T 7714
Zhang, Jing,Wang, Jian,Ma, Chengwei,et al. Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin[J]. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES,2020,21(8).
APA Zhang, Jing,Wang, Jian,Ma, Chengwei,&Lu, Junxia.(2020).Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin.INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES,21(8).
MLA Zhang, Jing,et al."Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin".INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 21.8(2020).
Files in This Item: Download All
File Name/Size DocType Version Access License
Related Services
Usage statistics
Scholar Google
Similar articles in Scholar Google
[Zhang, Jing]'s Articles
[Wang, Jian]'s Articles
[Ma, Chengwei]'s Articles
Baidu academic
Similar articles in Baidu academic
[Zhang, Jing]'s Articles
[Wang, Jian]'s Articles
[Ma, Chengwei]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Zhang, Jing]'s Articles
[Wang, Jian]'s Articles
[Ma, Chengwei]'s Articles
Terms of Use
No data!
Social Bookmark/Share
File name: 10.3390@ijms21082946.pdf
Format: Adobe PDF
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.