Figures & data
Figure 1. Transmission electron microscopy of collagen and HA-collagen fibrils reacted with Au-WGA, which could be bound specifically onto HA. (a) collagen; (b) HA-Collagen. (X100K) (arrows: nano particles bound to HA at a distance from collagen fibrils).
![Figure 1. Transmission electron microscopy of collagen and HA-collagen fibrils reacted with Au-WGA, which could be bound specifically onto HA. (a) collagen; (b) HA-Collagen. (X100K) (arrows: nano particles bound to HA at a distance from collagen fibrils).](/cms/asset/bf7b709c-4a58-425d-b5a8-78155af06aba/ianb19_a_420076_f0001_b.jpg)
Figure 2. Effect of feed HA/collagen ratio on the extents of surface immobilization by HA. The extent of HA immobilized on the collagen II fibrillar surface was estimated indirectly by the number of Au-WGA nanoparticles bound to fibrils. The number of bound Au-WGA, calculated from 100 TEM photo frames, increase with increasing amounts of reactant HA in the feed.
![Figure 2. Effect of feed HA/collagen ratio on the extents of surface immobilization by HA. The extent of HA immobilized on the collagen II fibrillar surface was estimated indirectly by the number of Au-WGA nanoparticles bound to fibrils. The number of bound Au-WGA, calculated from 100 TEM photo frames, increase with increasing amounts of reactant HA in the feed.](/cms/asset/9b62481f-8084-47ca-9f67-5a12396c4752/ianb19_a_420076_f0002_b.gif)
Figure 3. Topography of the collagen fibrils scanned with atomic force microscope. The scanning was conducted with tapping mode. (a) collagen, scan size = 2.5 µm; (b) HA-collagen, scan size = 1 µm.
![Figure 3. Topography of the collagen fibrils scanned with atomic force microscope. The scanning was conducted with tapping mode. (a) collagen, scan size = 2.5 µm; (b) HA-collagen, scan size = 1 µm.](/cms/asset/bffaa522-9582-4a2e-a04d-068b3af22926/ianb19_a_420076_f0003_b.jpg)