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Patterning Functional Proteins with High Selectivity for Biosensor Applications

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Zeitschriftentitel: JALA: Journal of the Association for Laboratory Automation
Personen und Körperschaften: Li, Nan, Ho, Chih-Ming
In: JALA: Journal of the Association for Laboratory Automation, 13, 2008, 4, S. 237-242
Format: E-Article
Sprache: Englisch
veröffentlicht:
SAGE Publications
Schlagwörter:
Medical Laboratory Technology
Computer Science Applications
author_facet Li, Nan
Ho, Chih-Ming
Li, Nan
Ho, Chih-Ming
author Li, Nan
Ho, Chih-Ming
spellingShingle Li, Nan
Ho, Chih-Ming
JALA: Journal of the Association for Laboratory Automation
Patterning Functional Proteins with High Selectivity for Biosensor Applications
Medical Laboratory Technology
Computer Science Applications
author_sort li, nan
spelling Li, Nan Ho, Chih-Ming 1535-5535 SAGE Publications Medical Laboratory Technology Computer Science Applications http://dx.doi.org/10.1016/j.jala.2008.04.001 <jats:p> In this article, two-dimensional hexamethyldisilazane (HMDS) micropatterns were generated on glass substrates using photolithographic techniques for the assembly of functional proteins. The non-HMDS patterned areas were backfilled with poly(ethylene glycol) (PEG) silane to reduce the nonspecific protein adsorption. The hydrophobic methyl-terminated HMDS monolayer was verified to be favorable for physical protein adsorption with bovine serum albumin (BSA). The PEG-silane derivatized surface significantly reduced the BSA nonspecific binding by 97% compared to the pristine glass substrate so that high patterning selectivity was achieved. A universal streptavidin template was generated using preadsorbed biotinylated BSA on HMDS surface to sequentially bind additional biotinylated antibodies. Using this patterning strategy, the biotinylated goat anti-mouse (biotin-GAM) antibodies can be specifically recognized by the fluorescently labeled mouse immunoglobulin G, which indicated that the immobilized biotin-GAM was still bioactive. Also, the immobilized alkaline phosphatase was demonstrated to retain its enzymatic functionality by the ability to convert its fluorogenic substrate fluorescein diphosphate into fluorescent products. This simple and effective protein patterning technique can also be extended to create nanoscale protein arrays. Additionally, its adaptability for the assembly of arbitrary proteins and antibodies provides great potentials for biosensor and biomicroelectromechanical systems (MEMS) applications. </jats:p> Patterning Functional Proteins with High Selectivity for Biosensor Applications JALA: Journal of the Association for Laboratory Automation
doi_str_mv 10.1016/j.jala.2008.04.001
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title Patterning Functional Proteins with High Selectivity for Biosensor Applications
title_unstemmed Patterning Functional Proteins with High Selectivity for Biosensor Applications
title_full Patterning Functional Proteins with High Selectivity for Biosensor Applications
title_fullStr Patterning Functional Proteins with High Selectivity for Biosensor Applications
title_full_unstemmed Patterning Functional Proteins with High Selectivity for Biosensor Applications
title_short Patterning Functional Proteins with High Selectivity for Biosensor Applications
title_sort patterning functional proteins with high selectivity for biosensor applications
topic Medical Laboratory Technology
Computer Science Applications
url http://dx.doi.org/10.1016/j.jala.2008.04.001
publishDate 2008
physical 237-242
description <jats:p> In this article, two-dimensional hexamethyldisilazane (HMDS) micropatterns were generated on glass substrates using photolithographic techniques for the assembly of functional proteins. The non-HMDS patterned areas were backfilled with poly(ethylene glycol) (PEG) silane to reduce the nonspecific protein adsorption. The hydrophobic methyl-terminated HMDS monolayer was verified to be favorable for physical protein adsorption with bovine serum albumin (BSA). The PEG-silane derivatized surface significantly reduced the BSA nonspecific binding by 97% compared to the pristine glass substrate so that high patterning selectivity was achieved. A universal streptavidin template was generated using preadsorbed biotinylated BSA on HMDS surface to sequentially bind additional biotinylated antibodies. Using this patterning strategy, the biotinylated goat anti-mouse (biotin-GAM) antibodies can be specifically recognized by the fluorescently labeled mouse immunoglobulin G, which indicated that the immobilized biotin-GAM was still bioactive. Also, the immobilized alkaline phosphatase was demonstrated to retain its enzymatic functionality by the ability to convert its fluorogenic substrate fluorescein diphosphate into fluorescent products. This simple and effective protein patterning technique can also be extended to create nanoscale protein arrays. Additionally, its adaptability for the assembly of arbitrary proteins and antibodies provides great potentials for biosensor and biomicroelectromechanical systems (MEMS) applications. </jats:p>
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author Li, Nan, Ho, Chih-Ming
author_facet Li, Nan, Ho, Chih-Ming, Li, Nan, Ho, Chih-Ming
author_sort li, nan
container_issue 4
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container_title JALA: Journal of the Association for Laboratory Automation
container_volume 13
description <jats:p> In this article, two-dimensional hexamethyldisilazane (HMDS) micropatterns were generated on glass substrates using photolithographic techniques for the assembly of functional proteins. The non-HMDS patterned areas were backfilled with poly(ethylene glycol) (PEG) silane to reduce the nonspecific protein adsorption. The hydrophobic methyl-terminated HMDS monolayer was verified to be favorable for physical protein adsorption with bovine serum albumin (BSA). The PEG-silane derivatized surface significantly reduced the BSA nonspecific binding by 97% compared to the pristine glass substrate so that high patterning selectivity was achieved. A universal streptavidin template was generated using preadsorbed biotinylated BSA on HMDS surface to sequentially bind additional biotinylated antibodies. Using this patterning strategy, the biotinylated goat anti-mouse (biotin-GAM) antibodies can be specifically recognized by the fluorescently labeled mouse immunoglobulin G, which indicated that the immobilized biotin-GAM was still bioactive. Also, the immobilized alkaline phosphatase was demonstrated to retain its enzymatic functionality by the ability to convert its fluorogenic substrate fluorescein diphosphate into fluorescent products. This simple and effective protein patterning technique can also be extended to create nanoscale protein arrays. Additionally, its adaptability for the assembly of arbitrary proteins and antibodies provides great potentials for biosensor and biomicroelectromechanical systems (MEMS) applications. </jats:p>
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spelling Li, Nan Ho, Chih-Ming 1535-5535 SAGE Publications Medical Laboratory Technology Computer Science Applications http://dx.doi.org/10.1016/j.jala.2008.04.001 <jats:p> In this article, two-dimensional hexamethyldisilazane (HMDS) micropatterns were generated on glass substrates using photolithographic techniques for the assembly of functional proteins. The non-HMDS patterned areas were backfilled with poly(ethylene glycol) (PEG) silane to reduce the nonspecific protein adsorption. The hydrophobic methyl-terminated HMDS monolayer was verified to be favorable for physical protein adsorption with bovine serum albumin (BSA). The PEG-silane derivatized surface significantly reduced the BSA nonspecific binding by 97% compared to the pristine glass substrate so that high patterning selectivity was achieved. A universal streptavidin template was generated using preadsorbed biotinylated BSA on HMDS surface to sequentially bind additional biotinylated antibodies. Using this patterning strategy, the biotinylated goat anti-mouse (biotin-GAM) antibodies can be specifically recognized by the fluorescently labeled mouse immunoglobulin G, which indicated that the immobilized biotin-GAM was still bioactive. Also, the immobilized alkaline phosphatase was demonstrated to retain its enzymatic functionality by the ability to convert its fluorogenic substrate fluorescein diphosphate into fluorescent products. This simple and effective protein patterning technique can also be extended to create nanoscale protein arrays. Additionally, its adaptability for the assembly of arbitrary proteins and antibodies provides great potentials for biosensor and biomicroelectromechanical systems (MEMS) applications. </jats:p> Patterning Functional Proteins with High Selectivity for Biosensor Applications JALA: Journal of the Association for Laboratory Automation
spellingShingle Li, Nan, Ho, Chih-Ming, JALA: Journal of the Association for Laboratory Automation, Patterning Functional Proteins with High Selectivity for Biosensor Applications, Medical Laboratory Technology, Computer Science Applications
title Patterning Functional Proteins with High Selectivity for Biosensor Applications
title_full Patterning Functional Proteins with High Selectivity for Biosensor Applications
title_fullStr Patterning Functional Proteins with High Selectivity for Biosensor Applications
title_full_unstemmed Patterning Functional Proteins with High Selectivity for Biosensor Applications
title_short Patterning Functional Proteins with High Selectivity for Biosensor Applications
title_sort patterning functional proteins with high selectivity for biosensor applications
title_unstemmed Patterning Functional Proteins with High Selectivity for Biosensor Applications
topic Medical Laboratory Technology, Computer Science Applications
url http://dx.doi.org/10.1016/j.jala.2008.04.001