Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/55459
Title: Guests mediated supramolecule-modified gold nanoparticles network for mimic enzyme application
Authors: Zhao, Jialin
Niu, Zhijuan
Huang, Xing
Hu, Xiaojun
Gao, Shouwei
Koh, Kwangnak
Chen, Hongxia
Keywords: Au-NP network;Glucose sensing;Para-sulfonatocalix[4]arene;Mimic enzyme;Nanoparticle assembly
Issue Date: Oct-2020
Publisher: NISCAIR-CSIR, India
Abstract: Supramolecules mediated porous metal nanostructures are meaningful materials because of their specific properties and wide range of applications. Here, we describe a general and simple strategy for building Au-networks based on the guest-induced 3D assembly of Au nanoparticles (Au-NPs) resulted in host-guest interaction resolved sulfonatocalix[4]arene (pSC4)-modified Au-NPs aggregate. The diverse guest molecules induced different porous network structures resulting in their different oxidize ability toward glucose. Among three different kinds of guest, hexamethylenediamine-pSC4-Au-NPs have high sensitivity, wide linear range and good stability. By surface characterization and calculating the electrochemical properties of the Au-NPs networks modified glassy carbon electrodes, the giving Au-NPs network reveals good porosity, high surface areas and increased conductance and electron transfer for the electrocatalysis. The synthesized nano-structures afford fast transport of glucose and ensure contact with a larger reaction surface due to high surface area. The fabricated sensor provides a platform for developing a more stable and efficient glucose sensor based on supramolecules mediated Au-NPs networks.
Page(s): 1434-1441
URI: http://nopr.niscair.res.in/handle/123456789/55459
ISSN: 0975-0975(Online); 0376-4710(Print)
Appears in Collections:IJC-A Vol.59A(10) [October 2020]

Files in This Item:
File Description SizeFormat 
IJCA 59A(10) 1434-1441.pdfMain Article1.02 MBAdobe PDFView/Open
IJCA 59A(10) 1434-1441_Suppl Data.pdfSupplementary Data516.49 kBAdobe PDFView/Open


Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.