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Amyloid-like amelogenin nanoribbons template mineralization via a low-energy interface of ion binding sites

Akkineni, Susrut ; Zhu, Cheng ; Chen, Jiajun ; Song, Miao ; Hoff, Samuel E. ; Bonde, Johan LU orcid ; Tao, Jinhui ; Heinz, Hendrik ; Habelitz, Stefan and De Yoreo, James J. (2022) In Proceedings of the National Academy of Sciences of the United States of America 119(19).
Abstract
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 β-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... (More)
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 β-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. (Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Amelogenin/chemistry, Amyloidogenic Proteins, Binding Sites, Calcium Phosphates, Dental Enamel Proteins, Nanotubes, Carbon
in
Proceedings of the National Academy of Sciences of the United States of America
volume
119
issue
19
article number
e2106965119
pages
10 pages
publisher
National Academy of Sciences
external identifiers
  • scopus:85129999810
  • pmid:35522709
ISSN
1091-6490
DOI
10.1073/pnas.2106965119
language
English
LU publication?
yes
id
6bee6d32-d9da-4fb7-a24b-3df329a23c6e
date added to LUP
2022-05-16 16:43:56
date last changed
2025-03-07 19:30:33
@article{6bee6d32-d9da-4fb7-a24b-3df329a23c6e,
  abstract     = {{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 β-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.}},
  author       = {{Akkineni, Susrut and Zhu, Cheng and Chen, Jiajun and Song, Miao and Hoff, Samuel E. and Bonde, Johan and Tao, Jinhui and Heinz, Hendrik and Habelitz, Stefan and De Yoreo, James J.}},
  issn         = {{1091-6490}},
  keywords     = {{Amelogenin/chemistry; Amyloidogenic Proteins; Binding Sites; Calcium Phosphates; Dental Enamel Proteins; Nanotubes, Carbon}},
  language     = {{eng}},
  month        = {{05}},
  number       = {{19}},
  publisher    = {{National Academy of Sciences}},
  series       = {{Proceedings of the National Academy of Sciences of the United States of America}},
  title        = {{Amyloid-like amelogenin nanoribbons template mineralization via a low-energy interface of ion binding sites}},
  url          = {{http://dx.doi.org/10.1073/pnas.2106965119}},
  doi          = {{10.1073/pnas.2106965119}},
  volume       = {{119}},
  year         = {{2022}},
}