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Conference Paper: Study of protein adsorption on polymer coatings surface by quartz crystal microbalance and electrochemical impedance methods

TitleStudy of protein adsorption on polymer coatings surface by quartz crystal microbalance and electrochemical impedance methods
Authors
KeywordsElectrochemical impedance
Ion-doped polyaniline modified electrode
Piezoelectric quartz crystal microbalance
Polyaniline modified electrode
SDS-doped polyaniline modified electrode
Issue Date2004
PublisherElsevier SA. The Journal's web site is located at http://www.elsevier.com/locate/snb
Citation
The 10th International Meeting on Chemical Sensors (IMCS-10), Tsukuba, Japan, 11-14 July 2004. In Sensors and Actuators, B: Chemical, 2004, v. 108 n. 1-2, p. 933-942 Abstract no. 3P064 How to Cite?
AbstractUnderstanding protein adsorption at electrode surface is important for biosensor development, in particular for piezoelectric quartz crystal (PQC) microbalance (QCM) sensor. Two proteins, bovine serum albumin (BSA) and fibrinogen were monitored in situ for their electrode-surface processes using both QCM and electrochemical impedance method. Conductive polymer films, which are based on de-doping polyaniline (PAN), ions-doped PAN (PAN + ClO 4 -) or sodium dodecyl sulfate (SDS) doped PAN (PAN + SDS) were prepared by electrochemical methods. The effect of the polymer film thickness and doping agents of PAN on protein adsorption were investigated. The maximum adsorptions of proteins onto PAN, PAN + ClO4 - and PAN + SDS films were measured, with results showing 0.71, 0.65 and 0.99 μg/cm2 for BSA and 2.73, 1.85 and 4.07 μg/cm2 for fibrinogen, respectively. The results suggest an end-on type adsorption of BSA to produce a mono-layered structure onto all three PAN films. As for fibrinogen, only the ClO4 --doped PAN film was adsorbed in an end-on type mono-layered structure. For the adsorption of fibrinogen on the other two PAN films, the adsorbed protein molecules formed multi-layered structure. The adsorption of proteins onto the PAN films was found to follow the Langmuir isotherm. Results from adsorption kinetics studies showed two consecutive steps in the adsorption of BSA and fibrinogen on PAN films. BSA and fibrinogen molecules were firstly adsorbed onto the films before undergone rearrangement. The adsorption equilibrium constants were 1.64 × 106, 9.51 × 105 and 2.42 × 106 for BSA adsorption and 2.74 × 108, 2. 43 × 108 and 2.52 × 108 for fibrinogen adsorption onto ClO4 --doped PAN, de-doping PAN and SDS-doped PAN films, respectively. © 2005 Published by Elsevier B.V.
DescriptionThese journal issues entitled: Proceedings of the Tenth International Meeting on Chemical Sensors (IMCS-10) 2004
Persistent Identifierhttp://hdl.handle.net/10722/69270
ISSN
2015 Impact Factor: 4.758
2015 SCImago Journal Rankings: 1.305
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhang, Y-
dc.contributor.authorFung, YS-
dc.contributor.authorYao, S-
dc.date.accessioned2010-09-06T06:12:07Z-
dc.date.available2010-09-06T06:12:07Z-
dc.date.issued2004-
dc.identifier.citationThe 10th International Meeting on Chemical Sensors (IMCS-10), Tsukuba, Japan, 11-14 July 2004. In Sensors and Actuators, B: Chemical, 2004, v. 108 n. 1-2, p. 933-942 Abstract no. 3P064-
dc.identifier.issn0925-4005en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69270-
dc.descriptionThese journal issues entitled: Proceedings of the Tenth International Meeting on Chemical Sensors (IMCS-10) 2004-
dc.description.abstractUnderstanding protein adsorption at electrode surface is important for biosensor development, in particular for piezoelectric quartz crystal (PQC) microbalance (QCM) sensor. Two proteins, bovine serum albumin (BSA) and fibrinogen were monitored in situ for their electrode-surface processes using both QCM and electrochemical impedance method. Conductive polymer films, which are based on de-doping polyaniline (PAN), ions-doped PAN (PAN + ClO 4 -) or sodium dodecyl sulfate (SDS) doped PAN (PAN + SDS) were prepared by electrochemical methods. The effect of the polymer film thickness and doping agents of PAN on protein adsorption were investigated. The maximum adsorptions of proteins onto PAN, PAN + ClO4 - and PAN + SDS films were measured, with results showing 0.71, 0.65 and 0.99 μg/cm2 for BSA and 2.73, 1.85 and 4.07 μg/cm2 for fibrinogen, respectively. The results suggest an end-on type adsorption of BSA to produce a mono-layered structure onto all three PAN films. As for fibrinogen, only the ClO4 --doped PAN film was adsorbed in an end-on type mono-layered structure. For the adsorption of fibrinogen on the other two PAN films, the adsorbed protein molecules formed multi-layered structure. The adsorption of proteins onto the PAN films was found to follow the Langmuir isotherm. Results from adsorption kinetics studies showed two consecutive steps in the adsorption of BSA and fibrinogen on PAN films. BSA and fibrinogen molecules were firstly adsorbed onto the films before undergone rearrangement. The adsorption equilibrium constants were 1.64 × 106, 9.51 × 105 and 2.42 × 106 for BSA adsorption and 2.74 × 108, 2. 43 × 108 and 2.52 × 108 for fibrinogen adsorption onto ClO4 --doped PAN, de-doping PAN and SDS-doped PAN films, respectively. © 2005 Published by Elsevier B.V.en_HK
dc.languageeng-
dc.publisherElsevier SA. The Journal's web site is located at http://www.elsevier.com/locate/snben_HK
dc.relation.ispartofSensors and Actuators, B: Chemical-
dc.subjectElectrochemical impedanceen_HK
dc.subjectIon-doped polyaniline modified electrodeen_HK
dc.subjectPiezoelectric quartz crystal microbalanceen_HK
dc.subjectPolyaniline modified electrodeen_HK
dc.subjectSDS-doped polyaniline modified electrodeen_HK
dc.titleStudy of protein adsorption on polymer coatings surface by quartz crystal microbalance and electrochemical impedance methods-
dc.typeConference_Paper-
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0924-4247&volume=108&spage=933&epage=942&date=2005&atitle=Study+of+protein+adsorption+on+polymer+coatings+surface+by+combining+quartz+crystal+microbalance+with+electrochemical+impedance+methodsen_HK
dc.identifier.emailFung, YS: ysfung@hku.hk-
dc.identifier.authorityFung, YS=rp00697-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.snb.2004.12.123en_HK
dc.identifier.scopuseid_2-s2.0-19744377798en_HK
dc.identifier.hkuros104147-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-19744377798&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume108-
dc.identifier.issue1-2-
dc.identifier.spage933-
dc.identifier.epage942-
dc.identifier.isiWOS:000230330300154-
dc.publisher.placeSwitzerlanden_HK
dc.identifier.scopusauthoridZhang, Y=7601310637en_HK
dc.identifier.scopusauthoridFung, Y=13309754700en_HK
dc.identifier.scopusauthoridSun, H=7404827538en_HK
dc.identifier.scopusauthoridZhu, D=7403599128en_HK
dc.identifier.scopusauthoridYao, S=35619833600en_HK
dc.customcontrol.immutablesml 150925-

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