Self-assembly and mineralization of full-length human amelogenin and its functional fragments
- Author:
Xiu ZHONG
1
;
Ting-Ting LAI
1
;
Liang CHEN
2
;
Kun TIAN
1
Author Information
- Publication Type:Journal Article
- Keywords: human amelogenin; leucine-rich amelogenin peptide; mineralization in vitro; self-assembly; tyrosine-rich amelogenin peptide
- MeSH: Amelogenin; Dental Enamel Proteins; Durapatite; Humans
- From: West China Journal of Stomatology 2021;39(4):419-424
- CountryChina
- Language:English
-
Abstract:
OBJECTIVES:To investigate the dynamic process of the self-assembly behaviors of a full-length human amelogenin (AM) and its functional fragments tyrosine-rich amelogenin peptide (TRAP) and leucine-rich amelogenin peptide(LRAP)
METHODS:The full-length human AM and its functional fragments, TRAP and LRAP, were reassembled and purified
RESULTS:When pH=8, the full-length human AM and TRAP assembly started spontaneously and formed "nanospheres" after 15 min.The nanospheres formed by TRAP existed independently, with a uniform size but without obvious internal structures. The full-length AM was assembled hierarchically, which formed "nanospheres" and further extended in all directions, formed a chain structure, and then aggregated into a net. The self-assembly behavior of LRAP was not obvious. Proteins mostly existed in the form of monomers without "nanosphere" formation. Only few oligomers were observed. The full-length AM was induced independently for 3 days to form rod-shaped HA crystals. TRAP and LRAP proteins were added, after 3 days the crystal elongation was obvious in the c axis, but the growth in plane A and plane B was poor.
CONCLUSIONS:The self-assembly and mineralization behaviors of full-length human AM, TRAP, and LRAP were consistent with the directional growth mechanism of HA crystals
