期刊
出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2106965119
关键词
beta-sheet; amelogenin; nucleation; scaffold; calcium phosphate
资金
- NIH/NIDCR [R01-DE025709, NSFOAC-1931587, NSFCMMI-1940335]
- NSF [ACI-1532236, ACI-1532235]
- DOE Office of Science user facility [DE-AC02-06CH11357]
Protein scaffolds and nanoribbons play a crucial role in the nucleation of amorphous calcium phosphate, which is important for the biomineralization of bones and teeth.
Protein scaffolds direct the organization of amorphous precursors that transform into mineralized tissues, but the templating mechanism remains elusive. Motivated by models for the biomineralization of tooth enamel, wherein amyloid-like amelogenin nanoribbons guide the mineralization of apatite filaments, we investigated the impact of nanoribbon structure, sequence, and chemistry on amorphous calcium phosphate (ACP) nucleation. Using full-length human amelogenin and peptide analogs with an amyloid-like domain, films of beta-sheet nanoribbons were self-assembled on graphite and characterized by in situ atomic force microscopy and molecular dynamics simulations. All sequences substantially reduce nucleation barriers for ACP by creating low-energy interfaces, while phosphoserines along the length of the nanoribbons dramatically enhance kinetic factors associated with ion binding. Furthermore, the distribution of negatively charged residues along the nanoribbons presents a potential match to the Ca-Ca distances of the multi-ion complexes that constitute ACP. These findings show that amyloid-like amelogenin nanoribbons provide potent scaffolds for ACP mineralization by presenting energetically and stereochemically favorable templates of calcium phosphate ion binding and suggest enhanced surface wetting toward calcium phosphates in general.
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