dc.contributor.author | Stair, Jacqueline L. | |
dc.contributor.author | Watkinson, Michael | |
dc.contributor.author | Krause, Steffi | |
dc.date.accessioned | 2013-01-14T08:59:03Z | |
dc.date.available | 2013-01-14T08:59:03Z | |
dc.date.issued | 2009-03-15 | |
dc.identifier.citation | Stair , J L , Watkinson , M & Krause , S 2009 , ' Sensor materials for the detection of proteases ' , Biosensors & Bioelectronics , vol. 24 , no. 7 , pp. 2113-2118 . https://doi.org/10.1016/j.bios.2008.11.002 | |
dc.identifier.issn | 0956-5663 | |
dc.identifier.uri | http://hdl.handle.net/2299/9601 | |
dc.description.abstract | The concept of generic and tunable sensor materials for the detection of proteases based on the thin film degradation of peptide cross-linked dextran hydrogels was explored. Hydrogel cross-links were formed via simple imine linkages between aldehyde groups in oxidized dextran and a peptide sequence susceptible to protease cleavage. Degradation of the hydrogel films was monitored in this study using a quartz crystal microbalance (QCM). The sensor material was developed using the protease/peptide pair of human neutrophil elastase (FINE) and Ala-Ala-Pro-Val-Ala-Ala-Lys (AAPVAAK). A direct relationship between the hydrogel degradation rate and protease activity was observed; HNE activities from 2.5 to 30 U ml(-1) were detected using 25% cross-linked films. Film degradation was rapid and was complete in less than 10 min for HNE activities >10 U ml(-1). An increase in the rate of degradation by a factor of 3.5 was achieved by increasing the cross-linking density from 25% to 75%. QCM admittance data fitted with a BVD equivalent circuit showed increases in film viscoelasticity upon enzyme addition. A second protease/peptide pair of cathepsin G and Ala-Ala-Pro-Phe-Phe-Lys (AAPFFK) was tested where 25% AAPFFK cross-linked hydrogels demonstrated a rapid response at 100 mU ml(-1). Swapping the protease/peptide pairs to HNE/AAPFFK and cathepsin G/AAPVAAK showed low levels of cross-sensitivity further demonstrating the specificity of film degradation. (C) 2008 Elsevier B.V. All rights reserved. | en |
dc.format.extent | 6 | |
dc.format.extent | 230474 | |
dc.language.iso | eng | |
dc.relation.ispartof | Biosensors & Bioelectronics | |
dc.subject | Protease | |
dc.subject | Enzymatic degradation | |
dc.subject | Peptide cross-linked hydrogel | |
dc.subject | Quartz crystal microbalance (QCM) | |
dc.subject | Human neutrophil elastase (HNE) | |
dc.subject | Cathepsin G | |
dc.subject | THIN POLYMER-FILMS | |
dc.subject | HUMAN-LEUKOCYTE ELASTASE | |
dc.subject | IMPEDANCE SPECTROSCOPY | |
dc.subject | PERIODONTAL-DISEASE | |
dc.subject | HOLOGRAPHIC SENSOR | |
dc.subject | CREVICULAR FLUID | |
dc.subject | CATHEPSIN-G | |
dc.subject | DEGRADATION | |
dc.subject | DEXTRAN | |
dc.subject | HYDROGELS | |
dc.title | Sensor materials for the detection of proteases | en |
dc.contributor.institution | School of Life and Medical Sciences | |
dc.contributor.institution | Nanopharmaceutics | |
dc.contributor.institution | Psychopharmacology, Drug Misuse and Novel Psychoactive Substances Unit | |
dc.contributor.institution | Centre for Hazard Detection and Protection Research | |
dc.contributor.institution | Centre for Research in Mechanisms of Disease and Drug Discovery | |
dc.contributor.institution | Department of Clinical, Pharmaceutical and Biological Science | |
dc.contributor.institution | Centre for Health Services and Clinical Research | |
dc.description.status | Peer reviewed | |
dc.identifier.url | http://www.scopus.com/inward/record.url?scp=60349126986&partnerID=8YFLogxK | |
rioxxterms.versionofrecord | 10.1016/j.bios.2008.11.002 | |
rioxxterms.type | Journal Article/Review | |
herts.preservation.rarelyaccessed | true | |