Redox Potential Dependence of Peptide Structure Studied Using Surface Enhanced Raman Spectroscopy

Michael A. Ochsenkuehn, Joanna A. Borek, Richard Phelps, Colin J. Campbell

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

We describe a novel surface enhanced Raman spectroscopy (SERS) sensing approach utilizing modified gold nanoshells and demonstrate its application to analysis of critical redox-potential dependent changes in antigen structure that are implicated in the initiation of a human autoimmune disease. In Goodpasture's disease, an autoimmune reaction is thought to arise from incomplete proteolysis of the autoantigen, alpha 3(IV)NC1(67-85) by proteases including Cathepsin D. We have used SERS to study conformational changes in the antigen that correlate with its oxidation state and to show that the antigen must be in the reduced state in order to undergo proteolysis. Our results demonstrate that a redox potential of similar to-200 mV was sufficient for reduction and subsequent productive processing of the antigenic fragment alpha 3(IV)NC1(67-85). Moreover, we demonstrate that the peptide bonds subsequently cleaved by Cathepsisn D can be identified by comparison with a SERS library of short synthetic peptides.

Original languageEnglish
Pages (from-to)2684-2688
Number of pages5
JournalNano Letters
Issue number7
Publication statusPublished - Jul 2011

Keywords / Materials (for Non-textual outputs)

  • SERS
  • nanoshell
  • peptide
  • redox
  • Goodpasture's
  • Proteolysis
  • CELL


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