Nanomedicine: Nanotechnology, Biology and Medicine
Volume 3, Issue 3 , Pages 192-197 , September 2007

Single-molecule selection and recovery of structure-specific antibodies using atomic force microscopy

  • Luda S. Shlyakhtenko, PhD

      Affiliations

    • Department of Pharmaceutical Sciences, College of Pharmacy, University of Nebraska Medical Center, Omaha, Nebraska, USA
  • ,
  • Bin Yuan, PhD

      Affiliations

    • Department of Chemical Engineering, Arizona State University, Tempe, Arizona, USA
  • ,
  • Sharareh Emadi, PhD

      Affiliations

    • Department of Chemical Engineering, Arizona State University, Tempe, Arizona, USA
  • ,
  • Yuri L. Lyubchenko, PhD, DSc

      Affiliations

    • Department of Pharmaceutical Sciences, College of Pharmacy, University of Nebraska Medical Center, Omaha, Nebraska, USA
  • ,
  • Michael R. Sierks, PhD

      Affiliations

    • Department of Chemical Engineering, Arizona State University, Tempe, Arizona, USA
    • Corresponding Author InformationCorresponding author. Michael R Sierks, Department of Chemical Engineering, Arizona State University, Box 876006, Tempe, AZ 85287-6006, USA.

Received 5 March 2007 ,Accepted 22 June 2007.

References 

  1. Hudson PJ, Souriau C. Engineered antibodies. Nat Med. 2003;9:129–134
  2. Dewey FM, MacDonald MM, Phillips SI, Priestley RA. Development of monoclonal-antibody-ELISA and -DIP-STICK immunoassays for Penicillium islandicum in rice grains. J Gen Microbiol. 1990;136:753–760
  3. Mendoza LG, McQuary P, Mongan A, et al. High-throughput microarray-based enzyme-linked immunosorbent assay (ELISA). Biotechniques 1999;27:778-80, 782-6, 8.
  4. Wang J. Electrochemical biosensors: towards point-of-care cancer diagnostics. Biosens Bioelectron. 2006;21:1887–1892
  5. Ferrari M. Cancer nanotechnology: opportunities and challenges. Nat Rev Cancer. 2005;5:161–171
  6. Hoogenboom HR. Selecting and screening recombinant antibody libraries. Nat Biotechnol. 2005;23:1105–1116
  7. Dobson CM. Protein misfolding, evolution and disease. Trends Biochem Sci. 1999;24:329–332
  8. McLaurin J, Yang D, Yip CM, Fraser PE. Review: modulating factors in amyloid-β fibril formation. J Struct Biol. 2000;130:259–270
  9. Dobson CM. Protein folding and its links with human disease. Biochem Soc Symp. 2001;68:1–26
  10. Perutz MF, Finch JT, Berriman J, Lesk A. Amyloid fibers are water-filled nanotubes. Proc Natl Acad Sci U S A. 2002;99:5591–5595
  11. Couzin J. Molecular biology. In yeast, prions' killer image doesn't apply. Science. 2002;297:758–761
  12. Bousset L, Briki F, Doucet J, Melki R. The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils. J Struct Biol. 2003;141:132–142
  13. Dobson CM. Principles of protein folding, misfolding and aggregation. Semin Cell Dev Biol. 2004;15:3–16
  14. Bucciantini M, et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 2002;416:507–511
  15. Kayed R, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science. 2003;300:486–489
  16. McAllister C, Karymov MA, Kawano Y, et al. Protein interactions and misfolding analyzed by AFM force spectroscopy. J Mol Biol. 2005;354:1028–1042
  17. Kransnoslobodtsev AV, Shlyakhtenko LA, Ukraintsev E, et al. Nanomedicine and protein misfolding diseases. Nanomedicine. 2005;1:300–305
  18. Lyubchenko YL, Sherman S, Shlyakhtenko LS, Uversky VN. Nanoimaging for protein misfolding and related diseases. J Cell Biochem. 2006;99:52–70
  19. Barkhordarian H, Emadi S, Schulz P, Sierks MR. Isolating recombinant antibodies against specific protein morphologies using atomic force microscopy and phage display technologies. Protein Eng Des Sel. 2006;19:497–502
  20. Emadi S, Liu R, Yuan B, et al. Inhibiting aggregation of α-synuclein with human single chain antibody fragments. Biochemistry. 2004;43:2871–2878
  21. Griffiths AD, Williams SC, Hartley O, et al. Isolation of high affinity human antibodies directly from large synthetic repertoires. EMBO J. 1994;13:3245–3260
  22. Zhou C, Emadi S, Sierks MR, Messer A. A human single-chain Fv intrabody blocks aberrant cellular effects of overexpressed α-synuclein. Mol Ther. 2004;10:1023–1031
  23. Marks JD, Griffiths AD, Malmqvist M, et al. By-passing immunization: building high affinity human antibodies by chain shuffling. Biotechnology. 1992;10:779–783
  24. Lyubchenko YL, Oden PI, Lampner D, et al. Atomic force microscopy of DNA and bacteriophage in air, water and propanol: the role of adhesion forces. Nucleic Acids Res. 1993;21:1117–1123
  25. Lyubchenko YL, Shlyakhtenko LS. Visualization of supercoiled DN with atomic force microscopy in situ. Proc Natl Acad Sci U S A. 1997;94:496–501
  26. Lyubchenko YL, Shlyakhtenko LS, Potaman VP, Sinden RR. Global and local DNA structure and dynamics. Single molecule studies with AFM. Microsc Microanal. 2002;8:170–171

 No conflict of interest was reported by the authors of this paper.

PII: S1549-9634(07)00086-X

doi: 10.1016/j.nano.2007.06.001

Nanomedicine: Nanotechnology, Biology and Medicine
Volume 3, Issue 3 , Pages 192-197 , September 2007