NDGA enhances the physicochemical and anti-biodegradation performance of dentin collagen.
collagen
crosslink
degradation
nordihydroguaiaretic acid
polyphenols
Journal
Oral diseases
ISSN: 1601-0825
Titre abrégé: Oral Dis
Pays: Denmark
ID NLM: 9508565
Informations de publication
Date de publication:
Nov 2023
Nov 2023
Historique:
revised:
31
10
2022
received:
06
09
2022
accepted:
24
11
2022
medline:
7
12
2023
pubmed:
29
11
2022
entrez:
28
11
2022
Statut:
ppublish
Résumé
Collagen fibrils from carious dentin matrix are prone to enzymatic degradation. This study investigates the feasibility and mechanism of nordihydroguaiaretic acid (NDGA), as a collagen crosslinker, to bio-modify the demineralized dentin matrix. The physicochemical properties of the crosslinked dentin matrix were characterized by swelling ratio, ninhydrin assay, Fourier Transform Infrared spectroscopy, and atomic force microscopy. The collagenase degradation resistance was evaluated by measuring loss of dry mass, hydroproline release, loss of elasticity, and micro-nano structure integrity. The cytotoxicity of NDGA-crosslinked dentin collagen was evaluated by flow cytometry. NDGA crosslinked dentin matrix without destroying the integrity of collagen. Mechanistically, NDGA formed bisquinone bond between two adjacent o-quinone groups, resulting in NDGA polymeric matrix in which collagen fibrils were embedded. NDGA modification could significantly enhance the stiffness of dentin matrix at macro-nano scale. The NDGA-crosslinked dentin matrix exhibited remarkably low collagen degradation and sustained bulk elasticity after collagenase challenge, which were attributed to decreased water content, physical masking of collagenase bind sites on collagen, and improved stiffness of collagen fibrils. Notably, NDGA-crosslinked dentin matrix exhibited excellent biocompatibility. NDGA, as a biocompatible collagen crosslinker, improves the mechanical properties and biodegradation resistance of demineralized dentin matrix.
Substances chimiques
Masoprocol
7BO8G1BYQU
Collagen
9007-34-5
Collagenases
EC 3.4.24.-
Types de publication
Journal Article
Langues
eng
Pagination
3525-3539Subventions
Organisme : National Natural Science Foundation of China
ID : 81771121
Organisme : National Natural Science Foundation of China
ID : 81871492
Organisme : National Natural Science Foundation of China
ID : 82230030
Organisme : Ten-Thousand Talents Program
ID : QNBJ2019-2
Organisme : Key R & D Plan of Ningxia Hui Autonomous Region
ID : 2020BCG01001
Organisme : Natural Science Foundation of Hubei Province
ID : 2021CFB367
Organisme : Innovative Research Team of High-level Local Universities in Shanghai
ID : SHSMU-ZLCX20212402
Organisme : New Clinical Techniques and Therapies of Peking University School and Hospital of Stomatology
ID : PKUSSNCT-13A01
Informations de copyright
© 2022 Wiley Periodicals LLC.
Références
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