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Robust Magnetized Graphene Oxide Platform for In Situ Peptide Synthesis and FRET-Based Protease Detection

Authors
Kim, SeongsooLee, Sang-MyungYoon, Je PilLee, NamhunChung, JinhyoChung, Woo-JaeShin, Dong-Sik
Issue Date
Sep-2020
Publisher
MDPI
Citation
SENSORS, v.20, no.18, pp 1 - 14
Pages
14
Journal Title
SENSORS
Volume
20
Number
18
Start Page
1
End Page
14
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/1233
DOI
10.3390/s20185275
ISSN
1424-8220
1424-3210
Abstract
Graphene oxide (GO)/peptide complexes as a promising disease biomarker analysis platform have been used to detect proteolytic activity by observing the turn-on signal of the quenched fluorescence upon the release of peptide fragments. However, the purification steps are often cumbersome during surface modification of nano-/micro-sized GO. In addition, it is still challenging to incorporate the specific peptides into GO with proper orientation using conventional immobilization methods based on pre-synthesized peptides. Here, we demonstrate a robust magnetic GO (MGO) fluorescence resonance energy transfer (FRET) platform based on in situ sequence-specific peptide synthesis of MGO. The magnetization of GO was achieved by co-precipitation of an iron precursor solution. Magnetic purification/isolation enabled efficient incorporation of amino-polyethylene glycol spacers and subsequent solid-phase peptide synthesis of MGO to ensure the oriented immobilization of the peptide, which was evaluated by mass spectrometry after photocleavage. The FRET peptide MGO responded to proteases such as trypsin, thrombin, and beta-secretase in a concentration-dependent manner. Particularly, beta-secretase, as an important Alzheimer's disease marker, was assayed down to 0.125 ng/mL. Overall, the MGO platform is applicable to the detection of other proteases by using various peptide substrates, with a potential to be used in an automated synthesis system operating in a high throughput configuration.
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공과대학 (화공생명공학부)
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