NDLI: AlGaN/GaN high electron mobility transistors for protein-peptide binding affinity study.

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AlGaN/GaN high electron mobility transistors for protein-peptide binding affinity study.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ren, Fan Chyi, Jen-Inn Hsu, You-Ren Wang, Yu-Lin Li, Sheng-Shian Lee, Geng-Yen Cheng, Hui-Teng Huang, Yu-Fen Sun, Yuh-Chang Chen, Chih-Chen Hsu, Chia-Hsien Huang, Chih-Cheng Hsu, Chen-Pin Yeh, J. Andrew Yao, Da-Jeng
Description	Author Affiliation: Huang CC ( Institute of Nanoengineering and Microsystems, National Tsing Hua University, Hsinchu, 300, Taiwan, ROC.)
Abstract	Antibody-immobilized AlGaN/GaN high electron mobility transistors (HEMTs) were used to detect a short peptide consisting of 20 amino acids. One-binding-site model and two-binding-site model were used for the analysis of the electrical signals, revealing the number of binding sites on an antibody and the dissociation constants between the antibody and the short peptide. In the binding-site models, the surface coverage ratio of the short peptide on the sensor surface is relevant to the electrical signals resulted from the peptide-antibody binding on the HEMTs. Two binding sites on an antibody were observed and two dissociation constants, 4.404×10(-11) M and 1.596×10(-9) M, were extracted from the binding-site model through the analysis of the surface coverage ratio of the short peptide on the sensor surface. We have also shown that the conventional method to extract the dissociation constant from the linear regression of curve-fitting with Langmuir isotherm equation may lead to an incorrect information if the receptor has more than one binding site for the ligand. The limit of detection (LOD) of the sensor observed in the experimental result (~10 pM of the short peptide) is very close to the LOD (around 2.7-3.4 pM) predicted from the value of the smallest dissociation constants. The sensitivity of the sensor is not only dependent on the transistors, but also highly relies on the affinity of the ligand-receptor pair. The results demonstrate that the AlGaN/GaN HEMTs cannot only be used for biosensors, but also for the biological affinity study.
ISSN	09565663
Volume Number	41
e-ISSN	18734235
Journal	Biosensors and Bioelectronics
Language	English
Publisher	Elsevier
Publisher Date	2013-03-15
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Aluminum Compounds Chemistry Antibodies Conductometry Instrumentation Gallium Immunoassay Peptides Protein Interaction Mapping Transistors, Electronic Binding Sites Biosensing Techniques Electron Transport Equipment Design Equipment Failure Analysis Protein Binding Reproducibility Of Results Sensitivity And Specificity Journal Article Research Support, Non-u.s. Gov't Discipline Biotechnology
Content Type	Text
Resource Type	Article
Subject	Nanoscience and Nanotechnology Medicine Biophysics Biomedical Engineering Biotechnology Electrochemistry

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