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- W2023358499 abstract "Noble metal nanoparticles arrays are well established substrates for surface enhanced Raman spectroscopy (SERS).Their ability to enhance optical fields is based on the interaction of their surface valence electrons with incidentelectromagnetic radiation. In the array configuration, noble metal nanoparticles have been used to produce SER spectralenhancements of up to 108 orders of magnitude, making them useful for the trace analysis of physiologically relevantanalytes such as proteins and peptides. Electrostatic interactions between proteins and metal surfaces result in thepreferential adsorption of positively charged protein domains onto metal surfaces. This preferential interaction has theeffect of disrupting the native conformation of the protein fold, with a concomitant loss of protein function. A majorhistoric advantage of Raman microspectroscopy has been is its non-invasive nature; protein denaturation on the metalsurfaces required for SER spectroscopy renders it a much more invasive technique. Further, part of the analytical powerof Raman spectroscopy lies in its use as a secondary conformation probe. The protein structural loss which occurs onthe metal surface results in secondary conformation readings which are not true to the actual native state of the analyte.This work presents a method for chemical fabrication of noble metal SERS arrays with surface immobilized layerswhich can protect protein native conformation without excessively mitigating the electromagnetic enhancements ofspectra. Peptide analytes are used as model systems for proteins. Raman spectra of alpha lactalbumin on surfaces andwhen immobilized on these novel arrays are compared. We discuss the ability of the surface layer to protect proteinstructure whilst improving signal intensity." @default.
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- W2023358499 date "2007-02-08" @default.
- W2023358499 modified "2023-09-23" @default.
- W2023358499 title "Noninvasive noble metal nanoparticle arrays for surface-enhanced Raman spectroscopy of proteins" @default.
- W2023358499 doi "https://doi.org/10.1117/12.725068" @default.
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