Analysis of matrix dynamics by atomic force microscopy

• Published in: Methods in Cell Biology Vol. 69; pp. 163 - 193
• Main Authors: Hansma, Helen G., Clegg, Dennis O., Kokkoli, Efrosini, Oroudjev, Emin, Tirrell, Matthew
• Format: Book Chapter Journal Article
• Language: English
• Published: United States Elsevier Science & Technology 2002
• Subjects: Aluminum Silicates; Animals; Basement Membrane - chemistry; Collagen - metabolism; Extracellular Matrix - chemistry; Extracellular Matrix - metabolism; Extracellular Matrix Proteins - chemistry; Extracellular Matrix Proteins - metabolism; Fibronectins - genetics; Fibronectins - metabolism; Gold - chemistry; Heparin - chemistry; Heparin - metabolism; Humans; Integrin alpha5beta1 - chemistry; Integrin alpha5beta1 - metabolism; Laminin - chemistry; Laminin - ultrastructure; Ligands; Macromolecular Substances; Microscopy, Atomic Force - instrumentation; Microscopy, Atomic Force - methods; Models, Molecular; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Tenascin - chemistry; Tenascin - metabolism
• ISBN: 0125441681; 9780125441681
• ISSN: 0091-679X
• DOI: 10.1016/S0091-679X(02)69012-0

This chapter describes matrix dynamics by atomic force microscopy (AFM). Matrix research is about biological surfaces, so the AFM, which investigates surfaces, is a good instrument for matrix research. The AFM images surfaces at resolutions between sub-nanometer to several nanometers and also senses the material properties of surfaces, through phase imaging in tapping mode AFM. Analysis of matrix dynamics for atomic force microscopy can be divided into three broad categories. First, AFM imaging in fluid has revealed dynamic processes such as the movements of laminin arms and the real-time degradation of collagen. Second, molecular force spectroscopy, also in fluid, has revealed intramolecular forces in the matrix protein tenascin and intermolecular forces between integrin and fibronectin. Third, AFM in air, the most common use of AFM for matrix analysis, has revealed static interactions among matrix macromolecules such as the binding sites of laminin and of human blood factor IX on collagen IV, and of heparin on fibronectin.