Scanning probe microscopy

Current Opinion in Chemical Biology

Volumn 1, Issue 3, 1997, Pages 370-377

  Colton, Richard J ^a   Baselt, David R ^a   Dufrêne, Yves F ^a   Green, John Bruce D ^a   Lee, Gil U ^a  

^a NAVAL RESEARCH LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC FORCE MICROSCOPY; CELL; CELL MEMBRANE; CHEMISTRY; CONFORMATION; INSTRUMENTATION; METHODOLOGY; PROTEIN CONFORMATION; REVIEW; VIRUS;

CELL MEMBRANE; CELLS; MICROSCOPY, ATOMIC FORCE; NUCLEIC ACID CONFORMATION; PROTEIN CONFORMATION; VIRUSES;

EID: 0031244215     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(97)80076-2     Document Type: Article

References (68)

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14. Thomson NH, Fritz M, Radmacher M, Cleveland JP, Schmidt CF, Hansma PK: Protein tracking and detection of protein motion using atomic force microscopy. Biophys J 1996, 70:2421-2431. An exciting new idea is presented to use the AFM to detect motions relevant to the biological functions of proteins.
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19. Proksch R, Lal R, Hansma PK, Morse D, Stucky G: Imaging the internal and external pore structure of membranes in fluid: Tapping-mode scanning ion conductance microscopy. Biophys J 1996, 71:2155-2157. This paper describes the construction of a combined scanning ion conductance microscope and an atomic force microscope that is sensitive to the surface topography and ionic conductance of synthetic membranes in an ionic solution.
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21. Hinterdorfer P, Baumgartner W, Gruber HJ, Schilcher K, Schindler H: Detection and localization of individual antibody-antigen recognition events by atomic force microscopy. Proc Natl Acad Sci USA 1996, 93:3477-3481. This paper gives exciting new results where the AFM is used to detect and map individual antibody-antigen recognition events between anti-human serum albumin mounted on the tip and human serum albumin attached to the surface of mica. The experiment simulates the ability of a probe to locate specific receptor sites on the surface of a biomembrane.
22. Baselt DR, Lee GU, Colton RJ: Biosensor based on force microscope technology. J Vac Sci Technol B 1996, 14:789-793. A ground breaking paper which shows how it may be possible to reduce the AFM laboratory experiment for measuring molecular recognition forces to a fieldable biosensor with single-molecule sensitivity.
23. Baselt DR, Lee GU, Hansen KM, Chrisey LA, Colton RJ: A high-sensitivity micromachined biosensor. Proc IEEE 1997, 85:672-680. A refinement on an earlier work (see Baselt et al., 1996; [22••]) in which the components of the AFM-based sensor are being optimized for a sensing application.
24. Roberts CJ, Davies MC, Tendler SJ, Williams PM, Davies J, Dawkes AC, Yearwood GD, Edwards JC: The discrimination of IgM and IgG type antibodies and Fab′ and F(ab)2 antibody fragments on an industrial substrate using scanning force microscopy. Ultramicroscopy 1996, 62:149-155.
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28. Rotsch C, Radmacher M: Mapping local electrostatic forces with the atomic force microscope. Langmuir 1997, 13:2825-2832. The nanometer-scale lateral resolution of the AFM is used to map electrostatic forces at an ampliphilic surface.
29. Radmacher M, Fritz M, Kacher CM, Cleveland JP, Hansma PK: Measuring the viscoelastic properties of human platelets with the atomic force microscope. Biophys J 1996, 70:556-567. A careful and elegant study in which atomic force microscopy force-distance curves are used to determine the elastic modulus of human platelets. This paper is an excellent example of how the AFM can be used to map topography and elasticity of biologically relevant systems.
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40. Mou J, Czajkowsky DM, Sheng SJ, Ho R, Shao Z: High resolution surface structure of E. coli GroES oligomer by atomic force microscopy. FEBS Lett 1996, 381:161-164.
41. Mou J, Sheng S, Ho R, Shao Z: Chaperonins GroEL and GroES: views from atomic force microscopy. Biophys J 1996, 71:2213-2221.
42. Kasas S, Thomson NH, Smith BL, Hansma HG, Zhu X, Guthold M, Bustamante C, Kool ET, Kashlev M, Hansma PK: Escherichia coli RNA polymerase activity observed using atomic force microscopy. Biochemistry 1997, 36:461-468. An outstanding piece of work which demonstrates the use of the AFM to follow biological processes such as the transcriptional activity of RNA polymerase at the molecular level. Now, if we can only sequence DNA at the rate of transcription.
43. Lyubchenko YL, Shlyakhtenko LS, Aki T, Adhya S: Atomic force microscopic demonstration of DNA looping by GaIR and HU. Nucleic Acids Res 1997, 25:873-876.
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48. Coury JE, McFail-Isom L, Williams LD, Bottomley LA: A novel assay for drug-DNA binding mode, affinity and exclusion number: scanning force microscopy. Proc Natl Acad Sci USA 1996, 93:12283-12286. An elegant experiment with vast ramifications in the area of drug development. The paper uses the AFM to directly monitor the length of DNA molecules as they are exposed to various concentrations of drugs. The data show clearly that the mode of drug binding to the DNA can be unambiguously determined in this way.
49. Wolfert MA, Seymour LW: Atomic force microscopic analysis of the influence of the molecular weight of poly(L)lysine on the size of polyelectrolyte complexes formed with DNA. Gene Ther 1996, 3:269-273.
50. McMaster TJ, Winfield MO, Baker AA, Karp A, Miles MJ: Chromosome classification by atomic force microscopy volume measurement. J Vac Sci Technol B 1996, 14:1438-1443. This approach will permit chromosomes to be identified and permit experiments to be performed on them without recourse to destructive chemical treatment.
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