SpringerProtocols: Abstract: ECM Macromolecules: Height-mapping and Nano-mechanics Using Atomic Force Microscopy

7. ECM Macromolecules: Height-mapping and Nano-mechanics Using Atomic Force Microscopy

By: Nigel W. Hodson, Cay M. Kielty, Michael J. Sherratt¹

Abstract

Full Text

Download PDF (550K)

The atomic force microscope (AFM) may be used to collect quantitative height data from extracellular matrix molecules and macro-molecular assemblies adsorbed to a wide range of solid substrates. The advantages of atomic force microscopy include rapid specimen preparation, which does not rely on chemical fixation, dehydration or heavy-metal staining, and sub-nanometre resolution imaging with a high signal–noise ratio. In combination with complimentary techniques such as molecular combing and by exploiting the ability to act as a force spectrometer, the AFM can provide valuable information on the nano-mechanical properties of extracellular matrix components.

Affiliation(s): (1) Faculty of Life Sciences, The Medical School, Stopford Building, The University of Manchester, Oxford Road, Manchester, M13 9PT, UK

Book Title: Extracellular Matrix Protocols: Second Edition

Series: Methods in Molecular Biology | Volume: 522 | Pub. Date: Jun-01-2008 | Page Range: 1-19 | DOI: 10.1007/978-1-59745-413-1_7

Subject: Cell Biology

Key Words: Atomic force microscopy - Fibrillin microfibrils - Type VI collagen microfibrils - Collagen fibrils - Fibronectin - Surface roughness - Surface amphiphilicity - Protein adsorption - Tip deconvolution

References

Download References

1.	Binnig, G. and Rohrer, H.(1982)Scanning tunnelling microscope. Helv. Phys. Acta55, 726–735.

2.	Eigler, D.M. and Schweizer, E.K.(1990)Positioning single atoms with a scanning tunneling microscope. Nature344, 524–526.

3.	Binnig, G., Quate, C.F. and Gerber, C.(1986)Atomic force microscope. Phys. Rev. Lett.56, 930–935.

4.	Zhong, Q., Inniss, D., Kjoller, K. and Ellings, V.B.(1993)Fractured polymer/silica fiber surface studied by tapping mode atomic force microscopy. Surf. Sci. Lett.290, L688–L692.

5.	Kasos, S., Gotzos, V. and Celio, M.R.(1993)Observation of living cells using the atomic force microscope. Biophys. J.64, 539–544.

6.	Fotiadis, D., Scheuring, S., Muller, S.A., Engel, A. and Muller, D.J.(2002)Imaging and manipulation of biological structures with the AFM. Micron33, 385–397.

7.	Bergkvist, M.,Carlsson, J. and Oscarsson, S.(2003)Surface-dependent conformations of human plasma fibronectin adsorbed to silica, mica, and hydrophobic surfaces, studied by Atomic Force Microscopy. J. Biomed. Mater.Res.64A, 349–356.

8.	Sherratt, M.J., Baldock, C., Haston, J.L., Holmes, D.F., Jones, C.J.P., Shuttleworth, C.A., Wess, T.J. and Kielty, C.M.(2003)Fibrillin microfibrils are stiff reinforcing fibres in compliant tissues. J. Mol. Biol.332, 183–193.

9.	Baldock, C., Sherratt, M.J., Shuttleworth, C.A. and Kielty, C.M.(2003)The supramolecular organization of collagen VI microfibrils. J. Mol. Biol.330, 297–307.

10.	Stephan, S., Sherratt, M.J., Hodson, N., Shuttleworth, C.A. and Kielty, C.M.(2004)Expression and supramolecular assembly of recombinant alpha 1(VIII) and alpha 2(VIII) collagen homotrimers. J. Biol. Chem.279, 21469–21477.

11.	Knupp, C., Pinali, C., Munro, P.M., Gruber, H.E., Sherratt, M.J., Baldock, C. and Squire, J.M.(2006)Structural correlation between collagen VI microfibrils and collagen VI banded aggregates. J. Struct. Biol.154, 312–326.

12.	Hernandez, J.C.R., Sanchez, M.S., Soria, J.M., Ribelles, J.L.G. and Pradas, M.M.(2007)Substrate chemistry-dependent conformations of single laminin molecules on polymer surfaces are revealed by the phase signal of atomic force microscopy. Biophys. J.93, 202–207.

13.	Sherratt, M.J., Bastrilles, J.Y., Bowden, J.J., Watson, R.E.B. and Griffiths, C.E.M.(2006)Age-related deterioration in the mechanical function of human dermal fibrillin microfibrils. Br. J. Dermatol.155, 240–241.

14.	Wang, H., Fertala, A., Ratner, B.D., Sage, E.H. and Jiang, S.Y.(2005)Identifying the SPARC binding sites on collagen I and procollagen I by atomic force microscopy. Anal. Chem.77, 6765–6771.

15.	Raspanti, M., Congui, T. and Guizzardi, S.(2001)Tapping-mode atomic force microscopy in fluid of hydrated extracellular matrix. Matrix Biol.20, 601–604.

16.	Cisneros, D.A., Hung, C., Franz, C.M. and Muller, D.J.(2006)Observing growth steps of collagen self-assembly by time-lapse high-resolution atomic force microscopy. J. Struct. Biol.154, 232–245.

17.	Lin, H., Clegg, D.O. and Lal, R.(1999)Imaging real-time proteolysis of single collagen I molecules with an atomic force microscope. Biochemistry38, 9956–9963.

18.	Sherratt, M.J., Holmes, D.F., Shuttleworth, C.A. and Kielty, C.M.(2004)Substrate-dependent morphology of supramolecular assemblies: fibrillin and type-VI collagen microfibrils. Biophys. J.86, 3211–3222.

19.	Garcia, A.J., Vega, M.D. and Boettiger, D.(1999)Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation. Mol. Biol. Cell.10, 785–798.

20.	Sherratt, M.J., Bax, D.V., Chaudhry, S.S., Hodson, N., Lu, J.R., Saravanapavan, P. and Kielty, C.M.(2005)Substrate chemistry influences the morphology and biological function of adsorbed extracellular matrix assemblies. Biomaterials26, 7192–7206.

21.	Bensimon, A., Simon, A., Chiffaudel, A., Croquette, V., Heslot, F. and Bensimon, D.(1994)Alignment and sensitive detection of DNA by a moving interface. Science265, 2096–2098.

22.	Tskhovrebova, L. and Trinick, J.(2001)Flexibility and extensibility in the titin molecule: analysis of electron microscope data. J. Mol. Biol.310, 755–771.

23.	Bustamante, C., Vesenka, J., Tang, C.L., Rees, W., Guthold, M. and Keller, R.(1992)Circular DNA molecules imaged in air by scanning force microscopy. Biochemistry31, 22–36.

24.	Engel, A., Schoenenberger, C.-A. and Muller, D.J.(1997)High resolution imaging of native biological sample surfaces using scanning probe microscopy. Curr. Opin. Struct. Biol.7, 279–284.

25.	Sherratt, M.J., Baldock, C., Morgan, A. and Kielty, C.M.(2007)The morphology of adsorbed extracellular matrix assemblies is critically dependent on solution calcium concentration. Matrix Biol.26, 156–166.

26.	Yang, Y., Wang, H. and Erie, D.A.(2003)Quantitative characterization of biomolecular assemblies and interactions using atomic force microscopy. Methods29, 175–187.

Comments (Loading...)

Post comment/View all comments