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Journal of Experimental Biology, Vol 202, Issue 21 3011-3020, Copyright © 1999 by Company of Biologists

JOURNAL ARTICLES

The supramolecular organisation of fibrillin-rich microfibrils determines the mechanical properties of bovine zonular filaments

DM Wright, VC Duance, TJ Wess, CM Kielty and PP Purslow
The Royal Veterinary and Agricultural University, Copenhagen, Denmark, School of Biosciences, Cardiff University, Cardiff CF1 3US, UK.

The zonular filaments from the eyes of cows are rich in microfibrils containing fibrillin. Tensile tests, stress-relaxation tests and X-ray diffraction studies were used to study the relationship between the mechanical behaviour of zonular filaments and the molecular packing and structure of the fibrillin-rich microfibrils. Zonular filaments show a non-linear (J-shaped) stress-strain curve and appreciable stress-relaxation. It is proposed that the non-linear properties are due to local variations in waviness in the microfibrils or assemblies of microfibrils, which straighten out and become more regularly aligned with strain. Previous and current X-ray diffraction results consistently show a partial ordering of microfibrils in zonular filaments into staggered aggregates which become more ordered and laterally aligned on stretching. Although the removal and re-addition of Ca(2+) is known to change the molecular structure of fibrillin, no effect was observed on the tensile properties of the zonular filaments. It is hypothesised that strain-induced deformation in the supramolecular aggregate packing may not be Ca(2+)-sensitive but could dominate the mechanical behaviour of microfibrillar arrays in zonular filaments.


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© The Company of Biologists Ltd 1999