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A more recent version of this article appeared on October 17, 2003
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M212854200v1
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Papers In Press, published online ahead of print July 21, 2003
J. Biol. Chem, 10.1074/jbc.M212854200
Submitted on December 17, 2002
Revised on July 21, 2003
Accepted on July 21, 2003

Raman microscopy and X-ray diffraction: A combined study of fibrillin-rich microfibrillar elasticity

J. Louise Haston, Søren B. Engelsen, Manfred Roessle, John Clarkson, Ewan W. Blanch, Clair Baldock, Cay M. Kielty, and Timothy J. Wess

Department of Biological Sciences, University of Stirling, Stirling FK9 4LA

Corresponding Author: j.l.haston{at}stir.ac.uk

Fibrillin-rich microfibrils are essential elastic structures contained within the extracellular matrix of a wide variety of connective tissues. Microfibrils are characterised as beaded filamentous structures with a variable axial periodicity (average 56 nm in the untensioned state), however the basis of their elasticity remains unknown. This study used a combination of small-angle X-ray scattering and Raman microscopy to investigate further the packing of microfibrils within the intact tissue and to determine the role of molecular reorganisation in the elasticity of these microfibrils. The application of relatively small strains produced no overall change in either molecular or macromolecular microfibrillar structure. In contrast, the application of larger tissue extensions (up to 150%) resulted in a markedly different structure, as observed by both Raman microscopy and small-angle X-ray scattering. These changes occurred at different levels of architecture and are interpreted as ranging from alterations in peptide bond conformation to domain rearrangement. This study demonstrates the importance of molecular elasticity in the mechanical properties of fibrillin-rich microfibrils in the intact tissue.


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