Amyloid-like amelogenin nanoribbons template mineralization via a low-energy interface of ion binding sites
Year: 2022
Type: article
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.
Language: English
Subfield: Biomaterials
Field: Materials Science
Domain: Physical Sciences
Open Access status: hybrid
Funders: National Science Foundation, U.S. Department of Energy, Battelle, Colorado State University, National Institutes of Health, Office of Science, University of Colorado Boulder, National Institute of General Medical Sciences, National Institute of Dental and Craniofacial Research, Division of Civil, Mechanical and Manufacturing Innovation, Biological and Environmental Research, Argonne National Laboratory
Awards: G102163711, G107546177, G1202769797, G125460123, G1286236842, G1313983767, G1337544421, G1414775356, G1581387393, G159716036, G1664757510, G1767990418, G1805209620, G1816284028, G1863003419, G1899721271, G223002938, G2287611682, G2506945562, G2510423872, G2539837713, G2603595557, G262962599, G2638771445, G2784524989, G2820049545, Amyloids in Enamel Development, G2857925935, G2911255433, G2972531269, G2988778103, G299733460, G2998698001, G3075337988, G3083819904, G3257500209, G334911014, G3432487278, G365575497, G382641700, G391136020, G409777406, G419881185, G42916606, G4333062023, G4501827968, G498139845, G513797252, G5175575554, G5373841109, G5607048534, G5653134238, G5726405315, G6173709932, G6188209572, G6206027980, G6652958823, G6848031779, G6918803902, Collaborative Research: I-AIM: Interpretable Augmented Intelligence for Multiscale Material Discovery, G7560550554, Collaborative Research: Frameworks: Cyberloop for Accelerated Bionanomaterials Design, G7787287669, G7799234019, G7912248388, G805243471, G821644656, G8229677252, G9000054807, G9000263589, ALS Efficiently Networking Advanced Beam Line Experiments (ALS-ENABLE), G921665476, G969889393, G993149817
OpenAlex ID: W4229002093