S. Yamamoto et al., ATOMIC-FORCE MICROSCOPIC STUDIES OF ISOLATED COLLAGEN FIBRILS OF THE BOVINE CORNEA AND SCLERA, Archives of histology and cytology, 60(4), 1997, pp. 371-378
Isolated collagen fibrils from the bovine cornea and sclera were inves
tigated by atomic force microscopy (AFM) in a non-contact mode. AFM im
aging visualized the surface topography of both corneal and scleral co
llagen fibrils with quantitative information on their height and width
. The corneal collagen fibrils had a height of 15.6+/-1.5 nm and a D-p
eriodicity of 63.9+/-0.5 nm. On the other hand, the height and D-perio
dicity of scleral collagen fibrils were 74.2+/-55.7 nm and 65.4+/-0.7
nm, respectively. A periodic banding pattern of grooves and ridges was
found in individual fibrils, although the groove depth was 2.81+/-0.2
9 nm in the cornea and 5.47+/-0.66 nm in the sclera, When collagen fib
rils were treated with acetic acid, they swelled and untwisted into su
bfibrils. The AFM is useful to analyze surface morphology of collagen
fibrils and their subfibrils at high resolution with quantitative info
rmation.