A high throughput method using electron microprobe analysis for quantification of protein adsorption on surfaces

Zhijun Bai; Trevor Byrne; M. J. Filiaggi; R. Sanderson; V. Chevrier; P. Stoffyn-Egli; J. R. Dahn

doi:10.1016/j.susc.2007.12.009

A high throughput method using electron microprobe analysis for quantification of protein adsorption on surfaces

Zhijun Bai, Trevor Byrne, M. J. Filiaggi, R. Sanderson, V. Chevrier, P. Stoffyn-Egli, J. R. Dahn

Medicine

Medicine

Résultat de recherche: Article › examen par les pairs

8 Citations (Scopus)

Résumé

Protein adsorption on solid surfaces can be easily and accurately quantified by electron microprobe analysis using wavelength dispersive spectroscopy (WDS) to detect the carbon and nitrogen atoms within the protein. The method was calibrated by measurements of the carbon and nitrogen WDS signals for sputtered carbon and C_0.72N_0.28 films of known mass per unit area. Fibrinogen adsorption isotherms on silicon wafers and sputtered Ni film samples were studied using this method. The sensitivities for fibrinogen are about 20 ng/cm² using carbon WDS, and about 60 ng/cm² using nitrogen WDS with a circular electron beam of 50 μm diameter. The fibrinogen adsorption results on Si and Ni are in agreement with reported values in the literature. This study suggests that WDS studies are a reliable way to rapidly and automatically screen metallic biomaterials, including combinatorial libraries, in a quantitative manner for their protein affinity.

Langue d'origine	English
Pages (de-à)	795-804
Nombre de pages	10
Journal	Surface Science
Volume	602
Numéro de publication	3
DOI	https://doi.org/10.1016/j.susc.2007.12.009
Statut de publication	Published - févr. 1 2008

Note bibliographique

Funding Information:
The financial support of Medtronic, Inc. (USA) is gratefully acknowledged. The authors would like to thank Dr. Russell Doolittle (University of California at San Diego) for information on the overall amino acid composition of fibrinogen.

ASJC Scopus Subject Areas

Condensed Matter Physics
Surfaces and Interfaces
Surfaces, Coatings and Films
Materials Chemistry

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10.1016/j.susc.2007.12.009

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title = "A high throughput method using electron microprobe analysis for quantification of protein adsorption on surfaces",

abstract = "Protein adsorption on solid surfaces can be easily and accurately quantified by electron microprobe analysis using wavelength dispersive spectroscopy (WDS) to detect the carbon and nitrogen atoms within the protein. The method was calibrated by measurements of the carbon and nitrogen WDS signals for sputtered carbon and C0.72N0.28 films of known mass per unit area. Fibrinogen adsorption isotherms on silicon wafers and sputtered Ni film samples were studied using this method. The sensitivities for fibrinogen are about 20 ng/cm2 using carbon WDS, and about 60 ng/cm2 using nitrogen WDS with a circular electron beam of 50 μm diameter. The fibrinogen adsorption results on Si and Ni are in agreement with reported values in the literature. This study suggests that WDS studies are a reliable way to rapidly and automatically screen metallic biomaterials, including combinatorial libraries, in a quantitative manner for their protein affinity.",

author = "Zhijun Bai and Trevor Byrne and Filiaggi, {M. J.} and R. Sanderson and V. Chevrier and P. Stoffyn-Egli and Dahn, {J. R.}",

note = "Funding Information: The financial support of Medtronic, Inc. (USA) is gratefully acknowledged. The authors would like to thank Dr. Russell Doolittle (University of California at San Diego) for information on the overall amino acid composition of fibrinogen.",

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AU - Bai, Zhijun

AU - Byrne, Trevor

AU - Filiaggi, M. J.

AU - Sanderson, R.

AU - Chevrier, V.

AU - Stoffyn-Egli, P.

AU - Dahn, J. R.

N1 - Funding Information: The financial support of Medtronic, Inc. (USA) is gratefully acknowledged. The authors would like to thank Dr. Russell Doolittle (University of California at San Diego) for information on the overall amino acid composition of fibrinogen.

PY - 2008/2/1

Y1 - 2008/2/1

N2 - Protein adsorption on solid surfaces can be easily and accurately quantified by electron microprobe analysis using wavelength dispersive spectroscopy (WDS) to detect the carbon and nitrogen atoms within the protein. The method was calibrated by measurements of the carbon and nitrogen WDS signals for sputtered carbon and C0.72N0.28 films of known mass per unit area. Fibrinogen adsorption isotherms on silicon wafers and sputtered Ni film samples were studied using this method. The sensitivities for fibrinogen are about 20 ng/cm2 using carbon WDS, and about 60 ng/cm2 using nitrogen WDS with a circular electron beam of 50 μm diameter. The fibrinogen adsorption results on Si and Ni are in agreement with reported values in the literature. This study suggests that WDS studies are a reliable way to rapidly and automatically screen metallic biomaterials, including combinatorial libraries, in a quantitative manner for their protein affinity.

AB - Protein adsorption on solid surfaces can be easily and accurately quantified by electron microprobe analysis using wavelength dispersive spectroscopy (WDS) to detect the carbon and nitrogen atoms within the protein. The method was calibrated by measurements of the carbon and nitrogen WDS signals for sputtered carbon and C0.72N0.28 films of known mass per unit area. Fibrinogen adsorption isotherms on silicon wafers and sputtered Ni film samples were studied using this method. The sensitivities for fibrinogen are about 20 ng/cm2 using carbon WDS, and about 60 ng/cm2 using nitrogen WDS with a circular electron beam of 50 μm diameter. The fibrinogen adsorption results on Si and Ni are in agreement with reported values in the literature. This study suggests that WDS studies are a reliable way to rapidly and automatically screen metallic biomaterials, including combinatorial libraries, in a quantitative manner for their protein affinity.

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A high throughput method using electron microprobe analysis for quantification of protein adsorption on surfaces

Résumé

Note bibliographique

ASJC Scopus Subject Areas

Accès au document

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