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Authors: P.C. Wuytens, H. Demol, N. Turk, K. Gevaert, A.G. Skirtach, M. Lamkanfi, R. Baets
Title: Gold Nanodome SERS platform for label-free detection of protease activity
Format: International Journal
Publication date: 8/2017
Journal/Conference/Book: Faraday Discussions
Editor/Publisher: Royal Society of Chemistry, 
Volume(Issue): 205(345) p.345-361
Location: United Kingdom
DOI: 10.1039/c7fd00124j
Citations: 9 (Dimensions.ai - last update: 17/1/2021)
6 (OpenCitations - last update: 4/1/2021)
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Abstract

Surface-enhanced Raman scattering provides a promising technology for sensitive and
selective detection of protease activity by monitoring peptide cleavage. Not only are
peptides and plasmonic hotspots similarly sized, Raman fingerprints also hold large potential
for spectral multiplexing. Here, we use a gold-nanodome platform for real-time detection
of trypsin activity on a CALNNYGGGGVRGNF substrate peptide. First, we investigate the
spectral changes upon cleavage through the SERS signal of liquid-chromatography
separated products. Next, we show that similar patterns are detected upon digesting
surface-bound peptides. We demonstrate that the relative intensity of the fingerprints from
aromatic amino acids before and after the cleavage site provides a robust figure of merit for
the turnover rate. The presented method offers a generic approach for measuring protease
activity, which is illustrated by developing an analogous substrate for endoproteinase Glu-C.

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