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High spatial resolution label-free detection of antigen-antibody binding on patterned surface by imaging ellipsometry

Graphical abstractQuantitatively study of the antibody/antigen interaction in surface area down to 32×32μm2 has been successfully achieved by high spatial resolution imaging ellipsometry. Highlights► Large area protein micro-arrays with feature size down to 8 × 8 μm2 square spots could be clearly im... Full description

Journal Title: Journal of Colloid And Interface Science August 15, 2011, Vol.360(2), p.826(8)
Main Author: Chang, Meng - Jie
Other Authors: Pang, Chao - Ran , Liu, Jun , Bai, Hua , Deng, Jun , Xu, Zhu - Guo , Zhang, Hao - Li
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0021-9797
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recordid: gale_ofa338860408
title: High spatial resolution label-free detection of antigen-antibody binding on patterned surface by imaging ellipsometry
format: Article
creator:
  • Chang, Meng - Jie
  • Pang, Chao - Ran
  • Liu, Jun
  • Bai, Hua
  • Deng, Jun
  • Xu, Zhu - Guo
  • Zhang, Hao - Li
subjects:
  • Antigens -- Chemical Properties
  • Surface Science -- Chemical Properties
  • Antibodies -- Chemical Properties
ispartof: Journal of Colloid And Interface Science, August 15, 2011, Vol.360(2), p.826(8)
description: Graphical abstractQuantitatively study of the antibody/antigen interaction in surface area down to 32×32μm2 has been successfully achieved by high spatial resolution imaging ellipsometry. Highlights► Large area protein micro-arrays with feature size down to 8 × 8 μm2 square spots could be clearly imaged by imaging ellipsometry. ► By using different patterns, 100-1600 label-free protein spots were imaged simultaneously. ► The thickness changes during the formation of protein patterns were quantitatively monitored on the 32 × 32 μm2 square spots. ► Quantitatively ellipsometric measurements were performed on protein arrays with densities above 5 × 104 spot/cm2. ► A single spot detection limit as low as 1.2 pg/spot was achieved. High spatial resolution and large area thickness mapping of label-free protein microarray has been achieved using imaging ellipsometry (IE) under optimized conditions. The protein patterns with feature size down to 8×8μm2 was readily imaged, and the binding between the surface immobilized antigen and the antibody was monitored. Quantitative thickness analysis of antibody–antigen binding on the 32×32μm2 micron spots was successfully performed, and we have obtained a limit of detection as low as 1.2pg/spot. This work demonstrates that appropriately optimized IE could be used as a highly sensitive and high through-put label-free technique for studying surface antigen–antibody recognition in sub-40μm scale.
language: English
source:
identifier: ISSN: 0021-9797
fulltext: fulltext
issn:
  • 0021-9797
  • 00219797
url: Link


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titleHigh spatial resolution label-free detection of antigen-antibody binding on patterned surface by imaging ellipsometry
creatorChang, Meng - Jie ; Pang, Chao - Ran ; Liu, Jun ; Bai, Hua ; Deng, Jun ; Xu, Zhu - Guo ; Zhang, Hao - Li
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descriptionGraphical abstractQuantitatively study of the antibody/antigen interaction in surface area down to 32×32μm2 has been successfully achieved by high spatial resolution imaging ellipsometry. Highlights► Large area protein micro-arrays with feature size down to 8 × 8 μm2 square spots could be clearly imaged by imaging ellipsometry. ► By using different patterns, 100-1600 label-free protein spots were imaged simultaneously. ► The thickness changes during the formation of protein patterns were quantitatively monitored on the 32 × 32 μm2 square spots. ► Quantitatively ellipsometric measurements were performed on protein arrays with densities above 5 × 104 spot/cm2. ► A single spot detection limit as low as 1.2 pg/spot was achieved. High spatial resolution and large area thickness mapping of label-free protein microarray has been achieved using imaging ellipsometry (IE) under optimized conditions. The protein patterns with feature size down to 8×8μm2 was readily imaged, and the binding between the surface immobilized antigen and the antibody was monitored. Quantitative thickness analysis of antibody–antigen binding on the 32×32μm2 micron spots was successfully performed, and we have obtained a limit of detection as low as 1.2pg/spot. This work demonstrates that appropriately optimized IE could be used as a highly sensitive and high through-put label-free technique for studying surface antigen–antibody recognition in sub-40μm scale.
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