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

Warren D. Marcus, Hongda Wang, Stuart Lindsay, Michael Sierks

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Fibrillar amyloid is the hallmark feature of many protein aggregation diseases, such as Alzheimer's and Parkinson's diseases. A monoclonal single-chain variable fragment (scFv) targeting insulin fibrils was isolated using phage display technology and an atomic force microscopy (AFM) mica substrate. Specific targeting of the scFv to insulin fibrils but not monomers or other small oligomeric forms, under similar conditions, was demonstrated both by enzyme-linked immunosorbent assays and AFM recognition imaging. The scFv also recognizes β-amyloid fibrils, a hallmark feature of Alzheimer's disease. The results suggest that the isolated scFv possibly targets a shared fibrillar motif-probably the cross-β-sheet characteristic of amyloid fibrils. The techniques outlined here provide additional tools to further study the process of fibril formation. The scFvs isolated can have potential use as diagnostic or therapeutic reagents for protein aggregation diseases.

Original languageEnglish (US)
Pages (from-to)1-7
Number of pages7
JournalNanomedicine: Nanotechnology, Biology, and Medicine
Volume4
Issue number1
DOIs
StatePublished - Mar 2008

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Single-Chain Antibodies
Atomic Force Microscopy
Insulin
Amyloid
Antibodies
Atomic force microscopy
Alzheimer Disease
Agglomeration
Proteins
Bacteriophages
Immunosorbents
Parkinson Disease
Mica
Enzyme-Linked Immunosorbent Assay
Technology
Assays
Enzymes
Monomers
Display devices
Imaging techniques

Keywords

  • Amyloid fibrils
  • Atomic force microscopy
  • Cross-β-sheet
  • Phage display
  • Single-chain variable fragment

ASJC Scopus subject areas

  • Molecular Biology
  • Molecular Medicine
  • Biotechnology
  • Biophysics
  • Medicine (miscellaneous)

Cite this

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