Abstract
The nature of the precise packing of collagen molecules into a collagen fibril, producing the characteristic regular banding, is still debatable. The problem has been approached using electron microscopy and X-ray diffraction techniques, and several models have been proposed, including hexagonal packing, an octafibril structure, a two-strand rope and a five-strand rope (for review, see ref. 1). For the past decade the pentafibrillar model, originally proposed by Smith2, has been widely accepted as the fundamental building unit. This model, based on the quarter-stagger end-overlap hypothesis of Hodge and Petruska3, was supported by the X-ray diffraction data of Miller and Wray4. These X-ray data have now been reinterpreted by Huhnes and Miller5 in terms of a quasi-hexagonal packing of collagen molecules. We argue here that until other characteristic parameters are taken into account, in particular the chemical cross-linking evidence, the packing problem is still unresolved.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Miller, A. in The Biochemistry of Collagen (eds Ramachandran, G. N. & Reddi, A. H.) (Academic, New York, 1976).
Smith, J. W. Nature 219, 157–159 (1968).
Hodge, A. J. & Petruska, J. A. in Aspects of Protein Structure (ed. Ramachandran, G. N.) 289–300 (Academic, New York, 1963).
Miller, A. & Wray, J. S. Nature 230, 437–439 (1971).
Hulmes, D. J. S. & Miller, A. Nature 282, 878–880 (1979).
McFarlane, E. F. Search 2, 171–172 (1971).
Rang, A. H. Biochemistry 11, 1828–1835 (1972).
Henkel, W., Rauterberg, J. & Stirtz, T. Eur. J. Biochem. 69, 223–231 (1976).
Miller, E.J. Biochem. biophys. Res. Commun. 45, 444–451 (1971).
Miller, E. J. & Robertson, P. B. Biochem. biophys. Res. Commun. 54, 432–439 (1973).
Nicholls, A. C. & Bailey, A. J. Biochem. J. 185, 195–201 (1980).
Henkel, W., Rauterberg, J. & Glanville, R. W. Eur. J. Biochem. 96, 249–256 (1979).
Light, N. D. & Bailey, A. J. Biochem. J. 185, 373–381 (1980).
Light, N. D. & Bailey, A. J. Biochem. J. 189, 111–124 (1980).
Parry, D. A. D. & Craig, A. S. Nature 282, 213–215 (1979).
Nemetschek, Th., Riedk, H. & Jonar, R. J. molec. Biol. 133, 67–83 (1979).
Squire, J. M. & Freundlich, A. Nature 288, 410–413 (1980).
Frazer, R. D. B., Macrae, T. P. & Suzuki, E. J. molec. Biol. 129, 463–481 (1979).
Trus, B. L. & Piez, K. A. Nature 286, 300–301 (1980).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Bailey, A., Light, N. & Atkins, E. Chemical cross-linking restrictions on models for the molecular organization of the collagen fibre. Nature 288, 408–410 (1980). https://doi.org/10.1038/288408a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/288408a0
- Springer Nature Limited
This article is cited by
-
Advanced application of collagen-based biomaterials in tissue repair and restoration
Journal of Leather Science and Engineering (2022)
-
Fluorescent nanonetworks: A novel bioalley for collagen scaffolds and Tissue Engineering
Scientific Reports (2014)
-
The mechanisms and consequences of the maturation and ageing of collagen
Proceedings / Indian Academy of Sciences (1999)
-
The chemistry of natural enzyme-induced cross-links of proteins
Amino Acids (1991)
-
Structure, function and ageing of the collagens of the eye
Eye (1987)