Characterization of the structural/properties correlation of crosslinked dentin collagen fibrils: AFM study

Amr S. Fawzy , Thong Beng Lu, Mah-Lee Ng

Research output: Chapter in Book/Conference paperChapterpeer-review

Abstract

Preservation of the structural integrity and mechanical properties of dentin collagen fibrils play an important role in the
determination of bond strength to dentin and the durability of bonded restorations. Enzymatic degradation of the dentin
collagen fibrils has been suggested as a possible mechanism responsible for adhesive bond failure. Collagen crosslinking
was suggested as a possible approach to increase the mechanical and structural stability and biodegradation resistance of
dentin collagen-matrix aiming to improve the durability of resin/dentin interfacial bond. Here we are presenting the use of
atomic force microscope (AFM) as a tool for characterizing and correlating the structural changes and the variations in
surface nano-mechanical properties of demineralized dentin collagen-matrix with collagenolytic challenges following
crosslinking with UVA-activated riboflavin. The AFM preliminary results showed that UVA-activated/riboflavin to be of
potential in enhancing the structural and mechanical stability of dentin collagen fibrils network against collagenolytic
challenges and further research are recommended.
Original languageEnglish
Title of host publicationCurrent Microscopy Contributions to Advances in Science and Technology
EditorsA Mendez-Vilas
Place of PublicationSpain
PublisherFormatex Research Center
Pages533-539
Number of pages7
ISBN (Print)9788493984359
Publication statusPublished - 2012
Externally publishedYes

Publication series

NameMicroscopy Book Series
Number1
Volume5

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