ABSTRACT The suprafibrillar organisation of collagen rich tissues is the keystone to the diversity of resultant structures made from relatively similar materials. The local organisation between fibrils may be essential to suprafibril structures that are critical to functionality such as transparency in cornea, where specific lateral relationships between fibrils dictate optical properties. Here we show that corneal X-ray diffraction combined with mechanical strains to disrupt a specific suprafibrillar relationship between fibrils evidence and a coherent staggered axial relationship between collagen fibrils. The data also shows evidence for auxetic behavior of the collagen fibrils and reveals a 120 nm diffraction feature previously unreported in collagen tissues. The results show that suprafibrillar organisation can be an essential component in tissue architecture that has hitherto been ignored, but now must be considered in mechanical and structural models.
Cite this paper
Patten, K. and Wess, T. (2013) Suprafibrillar structures of collagen, evidence for local organization and auxetic behaviour in architectures. Journal of Biophysical Chemistry, 4, 103-109. doi: 10.4236/jbpc.2013.43014.
 Traub, W., Arad, T. and Weiner, S. (1992) Growth of mineral crystals in turkey tendon collagen fibers. Connect Tissue Research, 28, 99-111.
 Wess, T.J., Purslow, P.P., Sherratt, M.J., Ashworth, J., Shuttleworth, C.A. and Kielty, C.M. (1998) Calcium Determines the supramolecular Organization of Fibrillinrich Microfibrils. The Journal of Cell Biology, 141, 829-837. doi:10.1083/jcb.141.3.829
 Fratzl, P. and Daxer, A. (1993) Structural transformation of collagen fibrils in corneal stroma during drying—An X-ray scattering study. Biophysical Journal, 64, 1210-1214. doi:10.1016/S0006-3495(93)81487-5
 Maurice, D.M. (1957) The structure and transparency of the cornea. The Journal of Physiology, 136, 263-286
 Meek, K.M. and Leonard, D.W. (1993) Ultrastructure of the corneal stroma: A comparative study. Biophysical Society, 64, 273-280. doi:10.1016/S0006-3495(93)81364-X
 Scott, J.E. and Thomlinson, A.M. (1998) The structure of interfibrillar proteoglycan bridges (shape modules) in extracellular matrix of fibrous connective tissues and their stability in various chemical environments. Journal of Anatomy, 192, 391-405.
 Wall, R.S., Elliott, G.F., Gyi, T.J., Meek, K.M. and Branford-White, C.J. (1988) Bovine corneal stoma contains a structural glycoprotein located in the gap region of the collagen fibrils. Bioscience Reports, 8, 77-83.
 Hodge, A.J. and Petruska, J.A. (1963) Recent studies with the electron microscope on ordered aggregates of the tropocollagen molecule. In: Ramachandran, G.N., Ed., Aspects of Protein Structure, Academic Press, New York, 289-300.
 Scott, J.E. and Haigh, M. (1985) Proteoglycan-type I collagen fibril interactions in bone and non-calcifying connective tissues. Bioscience Reports, 5, 71-81.
 Meek, K.M., Elliott, G.F. and Nave, C. (1986) A synchrotron X-ray diffraction study of bovine cornea stained with cupromeronic blue. Collagen Related Research 6, 203-218. doi:10.1016/S0174-173X(86)80026-7
 Wess, T.J., Purslow, P.P. and Kielty, C.M. (1998) X-ray diffraction studies of fibrillin-rich microfibrils: Effects of tissue extension on axial and lateral pack. Journal of Structural Biology, 122, 123-127.
 Holmes, D.F., Gilpin, C.J., Baldock, C., Ziese, U., Koster, A.J. and Kadler, K.E. (2001) Corneal collagen fibril structure in three dimensions: Structural insights into fibril assembly, mechanical properties, and tissue organisation. Proceedings of the National Academy of Sciences, 98, 7307-7312.
 Kern, P., Menasche, M. and Robert, L. (1991) Relative rates of biosynthesis of collagen type I, type V and type VI in calf cornea. Biochemistry, 274, 615-617.
 Keene, D.R., Lunstrum, G.P., Morris, N.P., Stoddard, D.W. and Burgeson, R.E. (1991) Two type XII-like collagens localize to the surface of banded collagen fibrils. The Journal of Cell Biology, 113, 971-978.