Seriation of Enzyme-Functionalized Multilayers for the Design of Scalable Biomimetic Mineralized Structures.
XRD
biomineralization
enamel
enzyme
layer‐by‐layer
Journal
Small (Weinheim an der Bergstrasse, Germany)
ISSN: 1613-6829
Titre abrégé: Small
Pays: Germany
ID NLM: 101235338
Informations de publication
Date de publication:
09 Sep 2024
09 Sep 2024
Historique:
revised:
23
07
2024
received:
18
03
2024
medline:
9
9
2024
pubmed:
9
9
2024
entrez:
9
9
2024
Statut:
aheadofprint
Résumé
Biomimetic hydroxyapatites are widely explored for their potential applications in the repair of mineralized tissues, particularly dental enamel, which is acellular and, thus, not naturally reformed after damage. Enamel is formed with a highly-controlled hierarchical structure, which is difficult to replicate up to the macroscale. A biomimetic approach is thus warranted, based on the same principles that drive biomineralization in vivo. Herein, a strategy for the design of enamel-like architectures is described, utilizing enzymes embedded in polyelectrolyte multilayers to generate inorganic phosphate locally, and provide a favorable chemical environment for the nucleation and growth of minerals. Moreover, a method is proposed to build up seriated mineral layers with scalable thicknesses, continuous mineral growth, and tunable morphology. Results show the outstanding growth of cohesive mineral layers, yielding macroscopic standalone fluoride and/or carbonate-substituted hydroxyapatite materials with comparable crystal structure and composition to native human mineralized tissues. This strategy presents a promising path forward for the biomimetic design of biomineral materials, particularly relevant for restorative applications, with an exquisite level of synthetic control over multiple orders of magnitude.
Identifiants
pubmed: 39246187
doi: 10.1002/smll.202402128
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2402128Subventions
Organisme : Institute of Materials Science (iMAT)
Organisme : Alliance Sorbonne Université
Organisme : FEDER European
Informations de copyright
© 2024 Wiley‐VCH GmbH.
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