Fig. 5
From: Synergistic strategy of riboflavin and lipoids to bioengineer resin dentin hybrid layer
(A) Display of scatter patterns and intensity vs. q-range plots for the dentin specimens modified with different adhesive treatments using SAXS. The colored graphical lines depict SAXS/WAXD patterns for collagen matrices (sizes and dispersion of fibrils) seen in controls, RF0.5%, RFLi0.5%/0.25%, RFLi0.5%/0.5%. The RF experimental groups displayed substantially larger changes within the patterns. The inset within the SAXS graphical streams show the deconvolved (blue profile) collected at a point representing deionised pattern of acquisition. The patterns represented (n = 2 per group) groups from control from the lowest intensity to higher intensities within no modification, RF0.5%, > RFLi0.5%/0.25%, > RFLi0.5%/0.5% (labeled). The shifts in X-ray diffraction peaks (black arrow) indicate changes in collagen fibril dimensions due to chemical changes and the crosslinking effect (p < 0.05) (D space of collagen fibril within RFLi0.5%/0.5%; yellow arrow). (B) The figure displays the most suitable positions assumed by the riboflavin molecule and lipoid as it is docked into collagen and enzymes (yellow arrow). The inset image pointed by yellow is the free radical oxidation by the presence of RF molecules. Schematic representation of the collagen network and the positioning of the simulation for an individual chain showing a simplified depiction of the collagen fibril network and the intermolecular cross-links connecting adjacent collagen molecules. The hydroxyproline residues of the molecule are denoted by fixed grey spheres. The blue and red denote the MD-modelled curves, corresponding to the colour scheme of amino acids and intramolecular hydrogen, respectively. The riboflavin binding mechanism has been confirmed to successfully bind to the catalytic sites of MMP-2 and −9 enzymes (white arrow). The blue, yellow and green ribbons resented when the enzyme’s active site was blocked by the crosslinking agent.
