Collagen molecules form the major part of tissues like bone, cornea or tendon where they organize into ordered fibrillar networks. The acid-soluble protein spontaneously assembles in liquid crystalline phases, characterized in polarized light microscopy and X-ray diffraction. Collagen fibrillogenesis obtained in condensed media establishes a link between the fibrillar networks described in vivo and the mesomorphic states obtained in vitro. Cell–matrix interactions on these biomimetic materials are currently analysed with perspectives in tissue engineering. In a morphogenetic context, we propose the hypothesis of a liquid crystalline order, between soluble precursor molecules, preceding fibrillogenesis.
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Giraud‐Guille et al. (2007) studied this question.
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