A peptide cross-linked polyacrylamide hydrogel for the detection of human neutrophil elastase

Polyacrylamide hydrogel films cross-linked with the peptide sequence AAPVAAK were synthesised on piezoelectric quartz crystals. Degradation of the hydrogel films was monitored using a combination of quartz crystal microbalance (QCM) and electrochemical impedance measurements. The films were shown to...

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Published in:Electrochimica Acta
Main Author: Kamarun D.; Zheng X.; Milanesi L.; Hunter C.A.; Krause S.
Format: Article
Language:English
Published: 2009
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-65749095562&doi=10.1016%2fj.electacta.2009.03.067&partnerID=40&md5=57eb07cf67522c814e5223c255727173
id 2-s2.0-65749095562
spelling 2-s2.0-65749095562
Kamarun D.; Zheng X.; Milanesi L.; Hunter C.A.; Krause S.
A peptide cross-linked polyacrylamide hydrogel for the detection of human neutrophil elastase
2009
Electrochimica Acta
54
22
10.1016/j.electacta.2009.03.067
https://www.scopus.com/inward/record.uri?eid=2-s2.0-65749095562&doi=10.1016%2fj.electacta.2009.03.067&partnerID=40&md5=57eb07cf67522c814e5223c255727173
Polyacrylamide hydrogel films cross-linked with the peptide sequence AAPVAAK were synthesised on piezoelectric quartz crystals. Degradation of the hydrogel films was monitored using a combination of quartz crystal microbalance (QCM) and electrochemical impedance measurements. The films were shown to degrade in the presence of human neutrophil elastase (HNE). The rate of degradation was directly related to the enzyme activity making the system suitable for the detection of HNE in the activity range from 0.72 to 30 U mL-1. The films were not affected by non-specific adsorption. Film degradation was only accompanied by changes in the QCM signal, while no significant impedance change was observed during degradation. © 2009 Elsevier Ltd. All rights reserved.

134686
English
Article
All Open Access; Green Open Access
author Kamarun D.; Zheng X.; Milanesi L.; Hunter C.A.; Krause S.
spellingShingle Kamarun D.; Zheng X.; Milanesi L.; Hunter C.A.; Krause S.
A peptide cross-linked polyacrylamide hydrogel for the detection of human neutrophil elastase
author_facet Kamarun D.; Zheng X.; Milanesi L.; Hunter C.A.; Krause S.
author_sort Kamarun D.; Zheng X.; Milanesi L.; Hunter C.A.; Krause S.
title A peptide cross-linked polyacrylamide hydrogel for the detection of human neutrophil elastase
title_short A peptide cross-linked polyacrylamide hydrogel for the detection of human neutrophil elastase
title_full A peptide cross-linked polyacrylamide hydrogel for the detection of human neutrophil elastase
title_fullStr A peptide cross-linked polyacrylamide hydrogel for the detection of human neutrophil elastase
title_full_unstemmed A peptide cross-linked polyacrylamide hydrogel for the detection of human neutrophil elastase
title_sort A peptide cross-linked polyacrylamide hydrogel for the detection of human neutrophil elastase
publishDate 2009
container_title Electrochimica Acta
container_volume 54
container_issue 22
doi_str_mv 10.1016/j.electacta.2009.03.067
url https://www.scopus.com/inward/record.uri?eid=2-s2.0-65749095562&doi=10.1016%2fj.electacta.2009.03.067&partnerID=40&md5=57eb07cf67522c814e5223c255727173
description Polyacrylamide hydrogel films cross-linked with the peptide sequence AAPVAAK were synthesised on piezoelectric quartz crystals. Degradation of the hydrogel films was monitored using a combination of quartz crystal microbalance (QCM) and electrochemical impedance measurements. The films were shown to degrade in the presence of human neutrophil elastase (HNE). The rate of degradation was directly related to the enzyme activity making the system suitable for the detection of HNE in the activity range from 0.72 to 30 U mL-1. The films were not affected by non-specific adsorption. Film degradation was only accompanied by changes in the QCM signal, while no significant impedance change was observed during degradation. © 2009 Elsevier Ltd. All rights reserved.
publisher
issn 134686
language English
format Article
accesstype All Open Access; Green Open Access
record_format scopus
collection Scopus
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