Archives of Histology and Cytology · 1997 · 49 citations · 11 references
Natural SciencesBioengineeringBiomedical EngineeringBiomechanicsMechanobiologyMicroscopic AnatomyAtomic Force MicroscopyBiomaterial Surface PropertiesCorneal AnatomyAtomic Force Microscopy AnalysisCollagen Fiber StructureCollagen Fibril DiameterCorneal Collagen OrganizationHigh-resolution ImagingNoncontact Atomic Force MicroscopyScleral Collagen OrganizationScleral Ultrastructure
Isolated collagen fibrils from the bovine cornea and sclera were investigated by atomic force microscopy (AFM) in a non-contact mode. AFM imaging visualized the surface topography of both corneal and scleral collagen 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-periodicity of 63.9 +/- 0.5 nm. On the other hand, the height and D-periodicity 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 +/- 0.29 nm in the cornea and 5.47 +/- 0.66 nm in the sclera. When collagen fibrils were treated with acetic acid, they swelled and untwisted into subfibrils. The AFM is useful to analyze surface morphology of collagen fibrils and their subfibrils at high resolution with quantitative information.
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G. Binnig, C. F. Quate, Ch. Gerber · Physical Review Letters · 1986 · 14.4K citations · Full text
Sequential assembly of collagen revealed by atomic force microscopy
Marla Gale, Michael S. Pollanen, Peter Markiewicz et al. · Biophysical Journal · 1995 · 96 citations · Full text