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J. Biol. Chem., Vol. 278, Issue 42, 41189-41197, October 17, 2003

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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 

From the Centre for Extracellular Matrix Biology, Department of Biological Sciences, University of Stirling, Stirling FK9 4LA, United Kingdom, ^¶Food Technology Centre for Advanced Food Studies, The Royal Veterinary and Agricultural University, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark, ^||European Synchrotron Radiation Facility, B.P. 220, F-38043 Grenoble Cedex, France, the ^**Department of Chemistry, Joseph Black Building, University of Glasgow, Glasgow G12 8QQ, Scotland, United Kingdom, the Department of Biomolecular Sciences UMIST, P. O. Box 88, Manchester M60 1QD, and Wellcome Trust Centre for Cell-Matrix Research, Schools of Biological Sciences and Medicine, University of Manchester, Oxford Road, Manchester M13 9PT, United Kingdom

Fibrillin-rich microfibrils are essential elastic structures contained within the extracellular matrix of a wide variety of connective tissues. Microfibrils are characterized 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 reorganization 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.

Received for publication, December 17, 2002 , and in revised form, June 12, 2003.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by Grant 98/S15326 from the Biotechnology and Biological Sciences Research Council. To whom correspondence should be addressed. Tel.: 44-1786-467814; Fax: 44-1786-464994; E-mail: j.l.haston{at}stir.ac.uk.

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