中大學術數位典藏-NCU Institutional Repository-提供博碩士論文、考古題、期刊論文、研究計畫等下載:Item 987654321/106535
English  |  正體中文  |  简体中文  |  全文筆數/總筆數 : 94274/94274 (100%)
造訪人次 : 82917827      線上人數 : 1884
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜尋範圍 查詢小技巧:
  • 您可在西文檢索詞彙前後加上"雙引號",以獲取較精準的檢索結果
  • 若欲以作者姓名搜尋,建議至進階搜尋限定作者欄位,可獲得較完整資料
  • 進階搜尋


    請使用永久網址來引用或連結此文件: https://ir.lib.ncu.edu.tw/handle/987654321/106535


    題名: AlGaN/GaN high electron mobility transistors for protein-peptide binding affinity study
    作者: 綦振瀛;Huang, Chih-Cheng;Lee, Geng-Yen;Chyi, Jen-Inn;Cheng, Hui-Teng;Hsu, Chen-Pin;Hsu, You-Ren;Hsu, Chia-Hsien;Huang, Yu-Fen;Sun, Yuh-Chang;Chen, Chih-Chen;Li, Sheng-Shian;Andrew Yeh, J.;Yao, Da-Jeng;Ren, Fan;Wang, Yu-Lin
    貢獻者: 資訊電機學院電機工程學系
    關鍵詞: Aluminum Compounds - chemistry;amino acids;antibodies;Antibodies - chemistry;Binding affinity;binding capacity;Binding Sites;Biological and medical sciences;Biosensing Techniques - instrumentation;biosensors;Biotechnology;Conductometry - instrumentation;detection limit;dissociation;Dissociation constants;Electron Transport;equations;Equipment Design;Equipment Failure Analysis;Fundamental and applied biological sciences. Psychology;Gallium - chemistry;GaN;High electron mobility transistors;Immunoassay - instrumentation;linear models;Peptides - chemistry;Protein Binding;Protein Interaction Mapping - instrumentation;Reproducibility of Results;Sensitivity and Specificity;Sensors;sorption isotherms;Transistors, Electronic
    日期: 2013-03-15
    上傳時間: 2026-04-23 13:27:08 (UTC+8)
    出版者: Elsevier Ltd.;Kidlington: Elsevier B.V
    摘要: 摘要: 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, 4.404×10−11M and 1.596×10−9M, 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 (∼10pM of the short peptide) is very close to the LOD (around 2.7–3.4pM) 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. ► AlGaN/GaN high electron mobility transistors detected a short peptide. ► Antibody immobilized on transistors bind the peptide to form a complex. ► Binding affinity of the complex was studied using binding-site models. ► Dissociation constants and the number of binding sites were revealed.
    其他題名: Biosens Bioelectron
    出版者: Kidlington: Elsevier B.V
    出版日期: 2013-03-15
    出處: Biosensors & bioelectronics, 2013-03, Vol.41, p.717-722
    版權: 2012 Elsevier B.V.
    版權: 2014 INIST-CNRS
    版權: Copyright © 2012 Elsevier B.V. All rights reserved.
    版權: Copyright © 2012 Elsevier B.V. Published by Elsevier B.V. All rights reserved. 2012 Elsevier B.V.
    識別號: ISSN: 0956-5663
    識別號: ISSN: 1873-4235
    識別號: EISSN: 1873-4235
    識別號: DOI: 10.1016/j.bios.2012.09.066
    識別號: PMID: 23102432
    顯示於類別:[電機工程學系] 期刊論文

    文件中的檔案:

    檔案 描述 大小格式瀏覽次數
    index.html0KbHTML27檢視/開啟


    在NCUIR中所有的資料項目都受到原著作權保護.

    社群 sharing

    ::: Copyright National Central University. | 國立中央大學圖書館版權所有 | 收藏本站 | 設為首頁 | 最佳瀏覽畫面: 1024*768 | 建站日期:8-24-2009 :::
    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - 隱私權政策聲明