Nonspecific-adsorption behavior of polyethylenglycol and bovine serum albumin studied by 55-MHz wireless-electrodeless quartz crystal microbalance

Ogi, Hirotsugu; Fukunishi, Yuji; Nagai, Hironao; Okamoto, Ken; Hirao, Masahiko; Nishiyama, Masayoshi

doi:https://doi.org/10.1016/j.bios.2009.03.035

Nonspecific-adsorption behavior of polyethylenglycol and bovine serum albumin studied by 55-MHz wireless-electrodeless quartz crystal microbalance

Ogi, Hirotsugu; Fukunishi, Yuji; Nagai, Hironao et al.

Biosensors and Bioelectronics, 2009, 24(10), 3148-3152

Number of Access:378（2025-11-25 02:19 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/84193

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Title	Nonspecific-adsorption behavior of polyethylenglycol and bovine serum albumin studied by 55-MHz wireless-electrodeless quartz crystal microbalance
Creator	NRID 1000090252626 1000090252626 researchmap permalink read0042771 read0042771 Scopus Author ID 35563683500 35563683500 ORCID 0000-0002-9602-5194 0000-0002-9602-5194 CreatorName Ogi, Hirotsugu
	CreatorName Fukunishi, Yuji
	CreatorName Nagai, Hironao
	CreatorName Okamoto, Ken
	NRID 1000080112027 1000080112027 CreatorName Hirao, Masahiko
	CreatorName Nishiyama, Masayoshi
Subject	Affinity
	Electrodeless
	Nonspecific adsorption
	QCM
Abstract	The nonspecific binding ability of polyethylenglycol (PEG) and bovine serum albumin (BSA) on modified and unmodified surfaces is quantitatively studied by a wireless-electrodeless quartz crystal microbalance (WE-QCM). PEG and BSA are important blocking materials in biosensors, but their affinities for proteins and uncoated substrates have not been known quantitatively. The WE-QCM allows quantitative analysis of the adsorption behavior of proteins on the electrodeless surfaces. Affinities of PEG, BSA, human immunoglobulin G (hIgG), and Staphylococcus protein A (SPA) for α-SiO2(quartz), Au thin film, PEG, and BSA are systematically studied by the homebuilt flow-injection system. PEG shows low affinities for the SiO2 surface (KA = 4.2 × 1 04 M-1) and the Au surface (KA = 6.6 × 1 04 M-1), but BSA shows higher affinity for the SiO2 surface (KA = 1.4 × 1 06 M-1). Both PEG and BSA show low affinities for hIgG (KA ∼ 1.5 × 1 05 M-1). However, the number of binding sites of PEG to hIgG is significantly larger than that of BSA, indicating that blocking for hIgG is favorably achieved by BSA, rather than PEG. © 2009 Elsevier B.V. All rights reserved.
Publisher	Elsevier B.V.
Source Title	Biosensors and Bioelectronics
Volume (Issue)	24(10)
Page	3148-3152
Date of Issued	2009-04-02
Language	English
Handle URL	https://hdl.handle.net/11094/84193
PISSN	09565663
NCID	AA10739666
NCID	AA1152282X
Relation.isVersionOf	DOI (Publisher Version) https://doi.org/10.1016/j.bios.2009.03.035
Relation.isIdenticalTo	PMID 19394213
Access Rights	open access
CopyRight	© 2009 Elsevier B.V. This manuscript version is made available under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
oaire:version	Accepted Manuscript
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Biosensors and Bioelectronics. 2009, 24(10), p. 3148-3152
DC.title	Nonspecific-adsorption behavior of polyethylenglycol and bovine serum albumin studied by 55-MHz wireless-electrodeless quartz crystal microbalance
DC.creator	Ogi, Hirotsugu
	Fukunishi, Yuji
	Nagai, Hironao
	Okamoto, Ken
	Hirao, Masahiko
	Nishiyama, Masayoshi
DC.publisher	Elsevier B.V.
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2009-04-02
DC.identifier	https://doi.org/10.1016/j.bios.2009.03.035
DC.subject	Affinity
	Electrodeless
	Nonspecific adsorption
	QCM
DCTERMS.abstract	The nonspecific binding ability of polyethylenglycol (PEG) and bovine serum albumin (BSA) on modified and unmodified surfaces is quantitatively studied by a wireless-electrodeless quartz crystal microbalance (WE-QCM). PEG and BSA are important blocking materials in biosensors, but their affinities for proteins and uncoated substrates have not been known quantitatively. The WE-QCM allows quantitative analysis of the adsorption behavior of proteins on the electrodeless surfaces. Affinities of PEG, BSA, human immunoglobulin G (hIgG), and Staphylococcus protein A (SPA) for α-SiO2(quartz), Au thin film, PEG, and BSA are systematically studied by the homebuilt flow-injection system. PEG shows low affinities for the SiO2 surface (KA = 4.2 × 1 04 M-1) and the Au surface (KA = 6.6 × 1 04 M-1), but BSA shows higher affinity for the SiO2 surface (KA = 1.4 × 1 06 M-1). Both PEG and BSA show low affinities for hIgG (KA ∼ 1.5 × 1 05 M-1). However, the number of binding sites of PEG to hIgG is significantly larger than that of BSA, indicating that blocking for hIgG is favorably achieved by BSA, rather than PEG. © 2009 Elsevier B.V. All rights reserved.
DC.rights	© 2009 Elsevier B.V. This manuscript version is made available under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
DC.format	84193
citation_title	Nonspecific-adsorption behavior of polyethylenglycol and bovine serum albumin studied by 55-MHz wireless-electrodeless quartz crystal microbalance
citation_author	Ogi, Hirotsugu
	Fukunishi, Yuji
	Nagai, Hironao
	Okamoto, Ken
	Hirao, Masahiko
	Nishiyama, Masayoshi
citation_publisher	Elsevier B.V.
citation_language	English
citation_date	2009-04-02
citation_journal_title	Biosensors and Bioelectronics
citation_volume	24
citation_issue	10
citation_firstpage	3148
citation_lastpage	3152
citation_doi	https://doi.org/10.1016/j.bios.2009.03.035
citation_pmid	19394213
citation_public_url	https://hdl.handle.net/11094/84193

Nonspecific-adsorption behavior of polyethylenglycol and bovine serum albumin studied by 55-MHz wireless-electrodeless quartz crystal microbalance

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