Abstract
Among biological macromolecules, collagen enjoys quite a peculiar status. Making up as much as a third of the protein fraction of the body it is the main responsible for the functional properties of the extracellular matrix, which can be efficiently tuned and tailored by modifying the length, volume fraction, and spatial layout of its collagen content. The supramolecular aggregates of collagen are therefore subject to be investigation by several viewpoints and at different scales, from the finest interactions of individual collagen molecules to the spatial layout of fibril bundles. As a consequence, no treatise can pretend to be exhaustive about the several techniques that can be useful in different moments and/or for different purposes. So, in this chapter, we focus only on some applications of the transmission electron microscope (TEM), of the scanning electron microscope (SEM), and of the atomic force microscope (AFM).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Chapman JA, Hulmes DJS (1984) Electron microscopy of the collagen fibril. In: Ruggeri A, Motta P (eds) Ultrastructure of the connective tissue matrix. Martinus Nijhoff, The Hague
Tzaphlidou M, Chapman JA, Al-Samman MH (1982) A study of positive staining for electron microscopy using collagen as a model system. II: staining by uranyl ions. Micron 13(2):133–145
Tzaphlidou M, Chapman JA, Meek KM (1982) A study of positive staining for electron microscopy using collagen as a model system. I: staining by phosphotungstate-tungstate ions. Micron 13(2):119–131
Tzaphlidou M (1988) Staining for electron microscopy by vanadyl sulphate. Use of collagen as a model system. Micron 19(3):141–145
Tzaphlidou M, Chapman JA (1986) A study of staining for electron microscopy using collagen as a model system. IV: phosphotungstate-tungstate negative staining patterns and their correlation with sequence data. Micron 17(3):269–280
Tzaphlidou M, Chapman JA (1987) A study of staining for electron microscopy using collagen as a model system. VI: Uranyl nitrate negative staining patterns and their correlation with sequence data. Micron 18(3):147–151
Ortolani F, Raspanti M, Marchini M (1991) Negative staining and genesis of D-periodicity in native collagen fibrils. Eur J Basic Appl Histochem 35:45–60
Ohtani O (1992) The maceration technique in scanning electron microscopy of collagen fiber frameworks: its application in the study of human livers. Arch Histol Cytol 55(Suppl):225–232
Raspanti M, Alessandrini A, Gobbi P et al (1996) Collagen fibril surface: TMAFM, FEG-SEM and Freeze-Etching observations. Microsc Res Tech 35:87–93
Stark M, Möller C, Müller DJ, Guckenberger R (2001) From images to interactions: High-resolution phase imaging in tapping-mode atomic force microscopy. Biophys J 80:3009–3018
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2019 Springer Science+Business Media, LLC, part of Springer Nature
About this protocol
Cite this protocol
Raspanti, M., Reguzzoni, M., Rita Basso, P., Protasoni, M., Martini, D. (2019). Visualizing the Supramolecular Assembly of Collagen. In: Vigetti, D., Theocharis, A.D. (eds) The Extracellular Matrix. Methods in Molecular Biology, vol 1952. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-9133-4_3
Download citation
DOI: https://doi.org/10.1007/978-1-4939-9133-4_3
Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-9132-7
Online ISBN: 978-1-4939-9133-4
eBook Packages: Springer Protocols