Redox Potential Dependence of Peptide Structure Studied Using Surface Enhanced Raman Spectroscopy
| Autor: | Richard G Phelps, Colin Campbell, Joanna Borek, Michael A. Ochsenkühn |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Collagen Type IV
Proteases Chemistry(all) Surface Properties Proteolysis Metal Nanoparticles Bioengineering Peptide Spectrum Analysis Raman Autoantigens Redox MOLECULES symbols.namesake Materials Science(all) Antigen Carbohydrate Conformation NANOPARTICLES medicine Humans Nanotechnology Peptide bond General Materials Science nanoshell CELL chemistry.chemical_classification Goodpasture's medicine.diagnostic_test SERS Chemistry Mechanical Engineering General Chemistry Surface-enhanced Raman spectroscopy Condensed Matter Physics peptide STATE Biochemistry redox symbols Biophysics Gold Peptides Raman spectroscopy Oxidation-Reduction |
| Zdroj: | Ochsenkuehn, M A, Borek, J A, Phelps, R & Campbell, C J 2011, ' Redox Potential Dependence of Peptide Structure Studied Using Surface Enhanced Raman Spectroscopy ', Nano Letters, vol. 11, no. 7, pp. 2684-2688 . https://doi.org/10.1021/nl200885p |
| ISSN: | 1530-6992 1530-6984 |
| DOI: | 10.1021/nl200885p |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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