Single probe nucleic acid immobilization on chemically modified single protein by controlling ionic strength and pH.

Single probe nucleic acid immobilization on chemically modified single protein by controlling ionic strength and pH. Research Abstract Details 

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Single probe nucleic acid immobilization on chemically modified single protein by controlling ionic strength and pH. Abstract Text:

Ryujiroh Yamasaki,Masateru Ito,BongKuk Lee,HoSup Jung,HeaYeon Lee,Tomoji Kawai,

In an effort toward determining the feasibility of single molecule analysis, we describe a case whereby the binding of one biotinylated DNA to one streptavidin molecule via electrostatic interactions was controlled by altering in pH 4.0-9.0 and 0.16 of the ion strength. The quantitative analysis of immobilized probe ssDNA was realized in real-time via a quartz crystal microbalance (QCM) and electrochemical (EC) measurement in the range 100 pM to 50 microM of probe oligonucleotide concentration. The variation amount of biotinylated ssDNA immobilized on the streptavidin-modified surface at pH 7.5 was about 0.16 pmol, giving a ratio of streptavidin to biotinylated ssDNA of about 1:1.1. On the other hand, at pH 4.9, it was immobilized about 0.29 pmol. From the shape of the Langmuir plot and QCM, the immobilization efficiency of biotinylated DNA via streptavidin at pH 4.9 was approximately twofold that at pH 7.5. In view points of the reaction velocity, it was increased with decreasing buffer solution pH, indicating a strong interaction of negatively charged probe DNA with the positively charged streptavidin. And also the EC response value of deltaI/I(streptavidin) for the immobilized biotinylated ssDNA in pH 4.9 was about 49%, while the corresponding value for the pH 7.5 was approximately 34%. As DNA molecules possess negative charges, electrostatic repulsion occurred between streptavidin and biotinylated ssDNA at pH 7.5. At pH 4.9, the attraction between the biotinylated ssDNA and streptavidin resulted in increased adsorption which has an isoelectric point of about 5.9. It was deduced that the binding of biotinylated ssDNA to one or two of the four binding sites of streptavidin can be controlled by adjusting the pH-controlled electrostatic interaction.

Single probe nucleic acid immobilization on chemically modified single protein by controlling ionic strength and pH. Publishing Authors By Initials

R Yamasaki,M Ito,B Lee,H Jung,H Lee,T Kawai,

For similar natural sciences: chemistry: chemistry, physical: surface properties research abstracts see: natural sciences: chemistry: chemistry, physical: surface properties research

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Single probe nucleic acid immobilization on chemically modified single protein by controlling ionic strength and pH. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Analytica chimica acta

VOLUME: 603

Page Numbers: 76-81

Journal Abbreviation: Anal. Chim. Acta

ISSN: 1873-4324

DAY: 21

MONTH: 09

YEAR: 2007

Single probe nucleic acid immobilization on chemically modified single protein by controlling ionic strength and pH. Information

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LANGUAGE: eng

NlmUniqueID: 370534

Single probe nucleic acid immobilization on chemically modified single protein by controlling ionic strength and pH. Keywords Mesh Terms:

KEYWORDS: Surface Properties

MESH TERMS: chemistry

Chemical & Substance for Abstract: Single probe nucleic acid immobilization on chemically modified single protein by controlling ionic strength and pH. Information

Substance Name: Streptavidin

Registry Number: 9013-20-1

Grant and Affiliation Information for Single probe nucleic acid immobilization on chemically modified single protein by controlling ionic strength and pH.

AFFILIATION: Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan.

Country: Netherlands

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MEDLINETA: Anal Chim Acta

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