Using atomic force microscopy, the self-assembly process of Type I collagen is followed at collagen concentrations from 0.5 to 100 �g/mL on muscovite mica, phlogopite mica, glass capillary tube, molybdenum disulfide (MoS2) and graphite. No fibril formation was found on MoS2 and graphite. The specific fibril patterns on mica surfaces are related to the mica crystal structure. The self-assembled collagen fibrils have a distribution of D-spacings, with an average value of 65-66 nm and a range between 55-70 nm. At 10 mg/mL, dense collagen fibrils form a gel in capillary tubes. When the gel from these glass capillary tubes is deposited on MoS2, they exhibit a D-spacing distribution similar to mica. The self-assembled collagen fibrils on various substrates showed similar D-spacing to those observed in biological tissues. This suggests Type I collagen assembly without heterotypic collagens or fibrillar cross-links is the origin of the D-spacing distribution.

In vitro self-assembly of type I collagen onto different substrates

245th National Meeting (2013)

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