Calcium interactions in amelogenin-derived peptide assembly

doi:10.3389/fphys.2022.1063970

	Calcium interactions in amelogenin-derived peptide assembly
	Zhang, Jing1,2,3 ; Bai, Yushi 4; Wang, Jian1 ; Li, Bing1 ; Habelitz, Stefan 4; Lu, Jun-xia1
	2022-12-14
发表期刊	FRONTIERS IN PHYSIOLOGY (IF:3.2[JCR-2023],4.0[5-Year])
EISSN	1664-042X
卷号	13
发表状态	已发表
DOI	10.3389/fphys.2022.1063970
摘要	Phosphorylation of serine residues has been recognized as a pivotal event in the evolution of mineralized tissues in many biological systems. During enamel development, the extracellular matrix protein amelogenin is most abundant and appears to be critical to the extreme high aspect ratios (length:width) of apatite mineral fibers reaching several millimeters in larger mammalian teeth. A 14-residue peptide (14P2, residues Gly8 to Thr21) was previously identified as a key sequence mediating amelogenin assembly formation, the domain also contains the native single phosphoserine residue (Ser16) of the full-length amelogenin. In this research, 14P2 and its phosphorylated form (p14P2) were investigated at pH 6.0 with various calcium and phosphate ion concentrations, indicating that both peptides could self-assemble into amyloid-like conformation but with differences in structural details. With calcium, the distance between P-31 within the p14P2 self-assemblies is averaged to be 4.4 & PLUSMN; 0.2 & ANGS;, determined by solid-state NMR P-31 PITHIRDS-CT experiments. Combining with other experimental results, solid-state Nuclear Magnetic Resonance (SSNMR) suggests that the p14P2 self-assemblies are in parallel in-register beta-sheet conformation and divalent calcium ions most likely connect two adjacent peptide chains by binding to the phosphate group of Ser16 and the carboxylate of Glu18 side-chain. This study on the interactions between calcium ions and amelogenin-derived peptides provides insights on how amelogenin may self-assemble in the presence of calcium ions in early enamel development.
关键词	amelogenin assembly mineral ions phosphorylation SSNMR
URL	查看原文
收录类别	SCI
语种	英语
资助项目	Natural Science Foundation of China["31770790","32171185"]
WOS研究方向	Physiology
WOS类目	Physiology
WOS记录号	WOS:000905124600001
出版者	FRONTIERS MEDIA SA
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/268687
专题	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_高性能计算平台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
通讯作者	Habelitz, Stefan; Lu, Jun-xia
作者单位	1.Shanghai Tech Univ, Sch Life Sci & Technol, Shanghai, Peoples R China 2.Univ Chinese Acad Sci, Beijing, Peoples R China 3.Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, CAS Ctr Excellence Mol Cell Sci, State Key Lab Mol Biol, Shanghai, Peoples R China 4.Univ Calif San Francisco, Sch Dent, Dept Preventat & Restorat Dent Sci, San Francisco, CA 94143 USA
第一作者单位	生命科学与技术学院
通讯作者单位	生命科学与技术学院
第一作者的第一单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Zhang, Jing,Bai, Yushi,Wang, Jian,et al. Calcium interactions in amelogenin-derived peptide assembly[J]. FRONTIERS IN PHYSIOLOGY,2022,13.
APA	Zhang, Jing,Bai, Yushi,Wang, Jian,Li, Bing,Habelitz, Stefan,&Lu, Jun-xia.(2022).Calcium interactions in amelogenin-derived peptide assembly.FRONTIERS IN PHYSIOLOGY,13.
MLA	Zhang, Jing,et al."Calcium interactions in amelogenin-derived peptide assembly".FRONTIERS IN PHYSIOLOGY 13(2022).