Nanomedicine: Nanotechnology, Biology and Medicine
Volume 4, Issue 1 , Pages 1-7 , March 2008

Characterization of an antibody scFv that recognizes fibrillar insulin and β-amyloid using atomic force microscopy

  • Warren D. Marcus, PhD

      Affiliations

    • Department of Physics and Astronomy, Arizona State University, Tempe, Arizona
    • Department of Chemical and Materials Engineering, Arizona State University, Tempe, Arizona
    • Corresponding Author InformationCorresponding author: Altor Bioscience Corporation, 2810 N Commerce Parkway, Miramar, Florida 33025, USA.
    • No longer at Arizona State University but all work performed while there.
  • ,
  • Hongda Wang, PhD

      Affiliations

    • Department of Physics and Astronomy, Arizona State University, Tempe, Arizona
  • ,
  • Stuart M. Lindsay, PhD

      Affiliations

    • Department of Physics and Astronomy, Arizona State University, Tempe, Arizona
    • The Biodesign Institute at Arizona State University, Arizona State University, Tempe, Arizona, USA
  • ,
  • Michael R. Sierks, PhD

      Affiliations

    • Department of Chemical and Materials Engineering, Arizona State University, Tempe, Arizona

Received 18 April 2007 ,Accepted 13 November 2007.

References 

  1. Stefani M. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim Biophys Acta. 2004;1739:5–25
  2. Ma QL, Lim GP, Harris-White ME, Yang F, Ambegaokar SS, Ubeda OJ, et al. Antibodies against β-amyloid reduce Aβ oligomers, glycogen synthase kinase-3β activation and tau phosphorylation in vivo and in vitro. J Neurosci Res. 2006;83:374–384
  3. Lee HJ, Khoshaghideh F, Patel S, Lee SJ. Clearance of α-synuclein oligomeric intermediates via the lysosomal degradation pathway. J Neurosci. 2004;24:1888–1896
  4. Tsai J, Grutzendler J, Duff K, Gan WB. Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches. Nat Neurosci. 2004;7:1181–1183
  5. Bouchard M, Zurdo J, Nettleton EJ, Dobson CM, Robinson CV. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 2000;9:1960–1967
  6. Clackson T, Hoogenboom HR, Griffiths AD, Winter G. Making antibody fragments using phage display libraries. Nature. 1991;352:624–628
  7. Marcus WD, Wang H, Lohr D, Sierks MR, Lindsay SM. Isolation of an scFv targeting BRG1 using phage display with characterization by AFM. Biochem Biophys Res Commun. 2006;342:1123–1129
  8. Stroh C, Wang H, Bash R, Ashcroft B, Nelson J, Gruber H, et al. Single-molecule recognition imaging microscopy. Proc Natl Acad Sci U S A. 2004;101:12503–12507
  9. Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev. 2001;81:741–766
  10. O'Nuallain B, Wetzel R. Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci U S A. 2002;99:1485–1490
  11. Chowdhury PS, Pastan I. Improving antibody affinity by mimicking somatic hypermutation in vitro. Nat Biotechnol. 1999;17:568–572
  12. McCall AM, Adams GP, Amoroso AR, Nielsen UB, Zhang L, Horak E, et al. Isolation and characterization of an anti-CD16 single-chain Fv fragment and construction of an anti-HER2/neu/anti-CD16 bispecific scFv that triggers CD16-dependent tumor cytolysis. Mol Immunol. 1999;36:433–445
  13. 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
  14. 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
  15. Emadi S, Barkhordarian H, Wang MS, Schulz P, Sierks MR. Isolation of a human single chain antibody fragment against oligomeric α-synuclein that inhibits aggregation and prevents α-synuclein-induced toxicity. J Mol Biol. 2007;368:1132–1144
  16. Wang H, Bash R, Yodh JG, Hager G, Lindsay SM, Lohr D. Using atomic force microscopy to study nucleosome remodeling on individual nucleosomal arrays in situ. Biophys J. 2004;87:1964–1971
  17. Wang H, Bash R, Yodh JG, Hager GL, Lohr D, Lindsay SM. Glutaraldehyde modified mica: a new surface for atomic force microscopy of chromatin. Biophys J. 2002;83:3619–3625
  18. Liu R, Barkhordarian H, Emadi S, Park CB, Sierks MR. Trehalose differentially inhibits aggregation and neurotoxicity of β-amyloid 40 and 42. Neurobiol Dis. 2005;20:74–81
  19. Phelan ML, Sif S, Narlikar GJ, Kingston RE. Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits. Mol Cell. 1999;3:247–253
  20. Bonar L, Cohen AS, Skinner MM. Characterization of the amyloid fibril as a cross-β protein. Proc Soc Exp Biol Med. 1969;131:1373–1375
  21. Antzutkin ON, Leapman RD, Balbach JJ, Tycko R. Supramolecular structural constraints on Alzheimer's β-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. Biochemistry. 2002;41:15436–15450
  22. Stromer T, Serpell LC. Structure and morphology of the Alzheimer's amyloid fibril. Microsc Res Tech. 2005;67:210–217

 The National Institutes of Health is acknowledged for funding this research through the minority postdoctoral supplement award.

 W.D. Marcus, H. Wang, S.M. Lindsay, M.R. Sierks, Characterization of an antibody scFv that recognizes fibrillar insuling and B-amyloid using atomic force microscopy. Nanomedicine: NMB 2008; 4: 1-6, doi: 10.1016/j.nano.2007.11.003.

PII: S1549-9634(07)00248-1

doi: 10.1016/j.nano.2007.11.003

Nanomedicine: Nanotechnology, Biology and Medicine
Volume 4, Issue 1 , Pages 1-7 , March 2008