Loughborough University
Leicestershire, UK
LE11 3TU
+44 (0)1509 263171
Loughborough University

Loughborough University Institutional Repository

Please use this identifier to cite or link to this item: https://dspace.lboro.ac.uk/2134/20728

Title: Detection of matrilysin (MMP-7) activity using polypeptide functionalized reduced graphene oxide field-effect transistor sensor.
Authors: Chen, Hu
Chen, Peng
Huang, Jingfeng
Selegard, Robert
Platt, Mark
Palaniappan, Alagappan
Aili, Daniel
Tok, Alfred I.Y.
Liedberg, Bo
Issue Date: 2016
Publisher: © American Chemical Society
Citation: CHEN, H. ... et al, 2016. Detection of matrilysin (MMP-7) activity using polypeptide functionalized reduced graphene oxide field-effect transistor sensor. Analytical chemistry, 88 (6), pp. 2994-2998.
Abstract: A novel approach for rapid and sensitive detection of matrilysin (MMP-7, a biomarker involved in the degradation of vari-ous macromolecules) based on polypeptide (JR2EC) functionalized reduced graphene oxide (rGO) field effect transistor (FET) is reported. MMP-7 specifically digests negatively charged JR2EC immobilized on rGO, thereby modulating the con-ductance of rGO-FET. The proposed assay enabled detection of MMP-7 at clinically relevant concentrations with a limit of detection (LOD) of 10 ng/mL (400 pM), attributed to the significant reduction of the net charge of JR2EC upon digestion by MMP-7. Quantitative detection of MMP-7 in human plasma was further demonstrated with a LOD of 40 ng/mL, illustrating the potential for the proposed methodology for tumor detection and carcinoma diagnostic (e.g. lung cancer and salivary gland cancer). Additionally, excellent specificity of the proposed assay was demonstrated using matrix metallopeptidase 1 (MMP-1), a protease of the same family. With appropriate selection and modification of polypeptides, the proposed assay could be extended for detections of other enzymes with polypeptide digestion capability.
Description: This paper is embargoed until February 2017
Sponsor: This research was funded by the Institute for Sports Research, Nanyang Technological University
Version: Accepted for publication
DOI: 10.1021/acs.analchem.5b04663
URI: https://dspace.lboro.ac.uk/2134/20728
Publisher Link: http://dx.doi.org/10.1021/acs.analchem.5b04663
ISSN: 0003-2700
Appears in Collections:Closed Access (Chemistry)

Files associated with this item:

File Description SizeFormat
acs%2Eanalchem%2E5b04663.pdfAccepted version987.96 kBAdobe PDFView/Open


SFX Query

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.