Raman Microscopy and X-ray Diffraction, a Combined Study of Fibrillin-rich Microfibrillar Elasticity
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Raman Microscopy and X-ray Diffraction, a Combined Study of Fibrillin-rich Microfibrillar Elasticity. / Haston, J. Louise; Engelsen, Søren B.; Roessle, Manfred; Clarkson, John; Blanch, Ewan W.; Baldock, Clair; Kielty, Cay M.; Wess, Timothy J.
I: Journal of Biological Chemistry, Bind 278, Nr. 42, 17.10.2003, s. 41189-41197.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Raman Microscopy and X-ray Diffraction, a Combined Study of Fibrillin-rich Microfibrillar Elasticity
AU - Haston, J. Louise
AU - Engelsen, Søren B.
AU - Roessle, Manfred
AU - Clarkson, John
AU - Blanch, Ewan W.
AU - Baldock, Clair
AU - Kielty, Cay M.
AU - Wess, Timothy J.
PY - 2003/10/17
Y1 - 2003/10/17
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0041571982&partnerID=8YFLogxK
U2 - 10.1074/jbc.M212854200
DO - 10.1074/jbc.M212854200
M3 - Journal article
C2 - 12876292
AN - SCOPUS:0041571982
VL - 278
SP - 41189
EP - 41197
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 42
ER -
ID: 306673465