English  |  正體中文  |  简体中文  |  Items with full text/Total items : 26987/38787
Visitors : 2289472      Online Users : 33
RC Version 4.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Adv. Search
LoginUploadHelpAboutAdminister

Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/38505

Title: Molecularly Imprinted Aptamers of Gold Nanoparticles for the Enzymatic Inhibition and Detection of Thrombin
Authors: Yu-Ju Liao;Yen-Chun Shiang;Chih-Ching Huang;Huan-Tsung Chang
Contributors: 國立臺灣海洋大學:生命科學暨生物科技學系
Date: 2012
Issue Date: 2016-09-08T02:03:33Z
Publisher: Langmuir
Abstract: We prepared thrombin-binding aptamer-conjugated gold nanoparticles (TBA–Au NPs) through a molecularly imprinted (MP) approach, which provide highly efficient inhibition activity toward the polymerization of fibrinogen. Au NPs (diameter, 13 nm), 15-mer thrombin-binding aptamer (TBA15) with different thymidine linkers, and 29-mer thrombin-binding aptamer (TBA29) with different thymidine linkers (Tn) in the presence of thrombin (Thr) as a template were used to prepare MP-Thr-TBA15/TBA29-Tn–Au NPs. Thrombin molecules were then removed from Au NPs surfaces by treating with 100 mM Tris-NaOH (pH ca. 13.0) to form MP-TBA15/TBA29-Tn–Au NPs. The length of the thymidine linkers and TBA density on Au NPs surfaces have strong impact on the orientation, flexibility, and stability of MP-TBA15/TBA29-Tn–Au NPs, leading to their stronger binding strength with thrombin. MP-TBA15/TBA29-T15–Au NPs (ca. 42 TBA15 and 42 TBA29 molecules per Au NP; 15-mer thymidine on aptamer terminal) provided the highest binding affinity toward thrombin with a dissociation constant of 5.2 × 10–11 M. As a result, they had 8 times higher anticoagulant (inhibitory) potency relative to TBA15/TBA29-T15–Au NPs (prepared in the absence of thrombin). We further conducted thrombin clotting time (TCT) measurements in plasma samples and found that MP-TBA15/TBA29-T15–Au NPs had greater anticoagulation activity relative to four commercial drugs (heparin, argatroban, hirudin, and warfarin). In addition, we demonstrated that thrombin induced the formation of aggregates from MP-TBA15-T15–Au NPs and MP-TBA29-T15–Au NPs, thereby allowing the colorimetric detection of thrombin at the nanomolar level in serum samples. Our result demonstrates that our simple molecularly imprinted approach can be applied for preparing various functional nanomaterials to control enzyme activity and targeting important proteins.
Relation: 28(24)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/38505
Appears in Collections:[生命科學系] 期刊論文

Files in This Item:

File Description SizeFormat
index.html0KbHTML75View/Open


All items in NTOUR are protected by copyright, with all rights reserved.

 


著作權政策宣告: 本網站之內容為國立臺灣海洋大學所收錄之機構典藏,無償提供學術研究與公眾教育等公益性使用,請合理使用本網站之內容,以尊重著作權人之權益。
網站維護: 海大圖資處 圖書系統組
DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback