TY - JOUR
T1 - Characterization of riboflavin-modified dentin collagen matrix
AU - Fawzy, A
AU - Nitisusanta, L
AU - Iqbal, K.
AU - Daood, U
AU - Beng, L T
AU - Neo, Jennifer
PY - 2012/11
Y1 - 2012/11
N2 - Crosslinking is considered a possible approach to increasing the mechanical and structural stability and biodegradation resistance of the dentin collagen matrix. The aim of this study was to investigate the mechanical and chemical variations and collagen degradation resistance associated with crosslinking of the dentin collagen matrix with UVA-activated riboflavin. Dentin collagen matrix specimens were treated with 0.1 and 1% riboflavin for 2 min and photo-activated with 7 mW/cm(2) UVA (368 nm) for 2 min. The structural change of the dentin collagen network with collagenase exposure was investigated by AFM and SEM at different time-points. The variations in surface/bulk mechanical properties and biodegradation resistance were characterized by nano-indentation, conventional mechanical testing, and hydroxyproline liberation at different time-points. Chemical changes associated with riboflavin/collagen-matrix interaction were analyzed by micro-Raman spectroscopy. UVA-activated riboflavin increased the mechanical properties, mechanical stability, and biodegradation resistance of the dentin collagen matrix. Higher collagen-network structural resistance against collagenolytic challenges was found with crosslinking. micro-Raman spectroscopy showed a strong dependency, in both intensity and wave-number, of certain Raman bands (1242-1667 cm(-1)) with crosslinking indicating the collagen/riboflavin interactions. UVA-activated riboflavin (1%) more efficiently crosslinked the dentin collagen matrix within a relatively clinically acceptable time-frame compared with 0.1% riboflavin.
AB - Crosslinking is considered a possible approach to increasing the mechanical and structural stability and biodegradation resistance of the dentin collagen matrix. The aim of this study was to investigate the mechanical and chemical variations and collagen degradation resistance associated with crosslinking of the dentin collagen matrix with UVA-activated riboflavin. Dentin collagen matrix specimens were treated with 0.1 and 1% riboflavin for 2 min and photo-activated with 7 mW/cm(2) UVA (368 nm) for 2 min. The structural change of the dentin collagen network with collagenase exposure was investigated by AFM and SEM at different time-points. The variations in surface/bulk mechanical properties and biodegradation resistance were characterized by nano-indentation, conventional mechanical testing, and hydroxyproline liberation at different time-points. Chemical changes associated with riboflavin/collagen-matrix interaction were analyzed by micro-Raman spectroscopy. UVA-activated riboflavin increased the mechanical properties, mechanical stability, and biodegradation resistance of the dentin collagen matrix. Higher collagen-network structural resistance against collagenolytic challenges was found with crosslinking. micro-Raman spectroscopy showed a strong dependency, in both intensity and wave-number, of certain Raman bands (1242-1667 cm(-1)) with crosslinking indicating the collagen/riboflavin interactions. UVA-activated riboflavin (1%) more efficiently crosslinked the dentin collagen matrix within a relatively clinically acceptable time-frame compared with 0.1% riboflavin.
KW - Adult
KW - Analysis of Variance
KW - Biotransformation
KW - Collagen/drug effects
KW - Cross-Linking Reagents/pharmacology
KW - Dental Bonding
KW - Dentin/drug effects
KW - Dentin Permeability/drug effects
KW - Dentin-Bonding Agents/chemistry
KW - Humans
KW - Hydroxyproline/analysis
KW - Microscopy, Atomic Force
KW - Microscopy, Electron, Scanning
KW - Molar
KW - Riboflavin/pharmacology
KW - Spectrum Analysis, Raman
KW - Surface Properties
KW - Tooth Demineralization
KW - Ultraviolet Rays
KW - Young Adult
U2 - 10.1177/0022034512459053
DO - 10.1177/0022034512459053
M3 - Article
C2 - 22914538
VL - 91
SP - 1049
EP - 1054
JO - Journal of Dental Research
JF - Journal of Dental Research
SN - 0022-0345
IS - 11
ER -