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Tuning bilayer twist using chiral counterious
Author(s) -
Oda Reiko,
Huc Yvan,
Schmutz Marc,
Candeau Sauveur,
Mackintosh Fred
Publication year - 1999
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/s0248-4900(99)90115-6
Subject(s) - humanities , art
Polarized light and electron transmisston microscopies have shown that in many biological tissues, for example compact bone. tendon, skin or cornea, the three-dimensional arratigements of the collagen fibrillar nerworks follow the same spatial distribution as those described in certain liquid crystals. How are such complex stmclures established in vivo ? A previous study using polarized light microscopy has demonstrated that in concentrated acidsnlubfe collagen solutions. monomers self-assemble into nemalic, precholesteric and ~cholesteric liquid crystals (Giraud-Guille M. M. (1992). J. MoL Bbl., 224, 861-873). Here we are studying the ability of procollagen. the soluble precursor oJ’ the collagen molecule, to &f-assemble inlo ordered phases. Typ I procollagen is purified from chick embryo tendons. and the final solution is concentrated between 5 and 30 m&J. Polarized light microscopy of viscous drops of procollagen in physiological buffer conditions reveals that molecules spontaneously evolve into nematic phases, precholesteric banded structures and prechoksteric cords. Rotary shadowing electron microscopy and electrophoresis testify that procollagen molecules are not promssed into cotlagen. Procollagen concentration is likely to be several tens of mg/mJ ill riv(? a$ in our in v&o preparations.These results suggest thl the lhreedimensional archilecture of collagen fibrillar network is governed by liquid crystalline assembly of procollagen molecules, along witi other components of the extracellular matrix, at a stage prior to lhe assembly of collagen fibrils.