• Spectroscopy and Spectral Analysis
  • Vol. 36, Issue 10, 3087 (2016)
CHEN Lei1、2, KONG Wei-he1, HAN Xiao-xia2, and ZHAO Bing2
Author Affiliations
  • 1[in Chinese]
  • 2[in Chinese]
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    DOI: 10.3964/j.issn.1000-0593(2016)10-3087-05 Cite this Article
    CHEN Lei, KONG Wei-he, HAN Xiao-xia, ZHAO Bing. Study of Proteins Based on Surface-Enhanced Raman Spectroscopy (SERS)[J]. Spectroscopy and Spectral Analysis, 2016, 36(10): 3087 Copy Citation Text show less

    Abstract

    This article outlines the recent progress in surface enhanced Raman spectroscopy (SERS) based proteins applications. SERS is a specific Raman spectroscopic technique that provides enhanced Raman signals (several orders of magnitude greater than normal) for numerous Raman-active analyte molecules adsorbed onto rough metal surfaces. SERS is a sensitive, selective, and versatile technique that lends to fast data acquisition in actual time. Therefore, SERS has undergone rapid development because of its technical advantages in instrumentation, data analysis methods and its multiple biological applications. This article highlights several representative areas in proteins where SERS could be employed. Some of the proteins applications of SERS are more maturely developed, whereas others are in their initial stages of development (in laboratories). This article discusses the recent developments in SERS based quantitative analysis: directly with different substrates (e.g. biomolecules on electrodes, colloidal particles, and periodic pattern structure and tip based substrates). Furthermore, SERS based techniques are advantageous for obtaining valuable information on protein-protein, protein-ligand, and protein-drug recognitions via spectral differences among molecular bridges. SERS based techniques show considerable promise for qualitative and/or quantitative analyses of biological systems.
    CHEN Lei, KONG Wei-he, HAN Xiao-xia, ZHAO Bing. Study of Proteins Based on Surface-Enhanced Raman Spectroscopy (SERS)[J]. Spectroscopy and Spectral Analysis, 2016, 36(10): 3087
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