Self-assembly and mineralization of full-length human amelogenin and its functional fragments / 华西口腔医学杂志
West China Journal of Stomatology
;
(6): 419-424, 2021.
Article
in English
| WPRIM
| ID: wpr-887753
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
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Durapatite
/
Dental Enamel Proteins
/
Amelogenin
Limits:
Humans
Language:
English
Journal:
West China Journal of Stomatology
Year:
2021
Type:
Article
Similar
MEDLINE
...
LILACS
LIS