Conjugated polymers nanostructured as smart interfaces for controlling the catalytic properties of enzymes

被引:27
作者
Barbosa, Camila Gouveia [1 ]
Caseli, Luciano [1 ]
Peres, Laura Oliveira [1 ]
机构
[1] Univ Fed Sao Paulo, Lab Hybrid Mat, Diadema, SP, Brazil
基金
巴西圣保罗研究基金会;
关键词
Conjugated polymer; Urease; Langmuir-Blodgett; Enzyme activity; Biosensor; LANGMUIR-BLODGETT-FILMS; HORSERADISH-PEROXIDASE; BIOSENSOR DEVELOPMENT; UREASE; SENSOR; IMMOBILIZATION;
D O I
10.1016/j.jcis.2016.05.033
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The search for new molecular architectures to improve the efficiency of enzymes entrapped in ultrathin films is useful to enhance the effectiveness of biosensors. In this present work, conjugated polymers, based on thiophene and fluorine, were investigated to verify their suitability as matrices for the immobilization of urease. The copolymer poly[(9,9-dioctylfluorene)-co-thiophene], PDOF-co-Th was spread on the air-water interface forming stable Langmuir monolayers as determined by surface pressure-area isotherms, polarization-modulation reflection-absorption infrared spectroscopy (PM-IRRAS), and Brewster angle microscopy (BAM). Urease was incorporated in the floating monolayers being further transferred to solid supports as mixed Langmuir-Blodgett (LB) films. These films were then characterized with transfer ratio, fluorescence spectroscopy, PM-IRRAS and atomic force microscopy, confirming the co-transfer of the enzyme as well as its structuring in beta-sheets. The catalytic activity was detected for urease, with a lower reaction rate than that encountered for the homogeneous environment. This was attributed to conformational constraints imposed to the biomacromolecule entrapped in the polymeric matrix. (C) 2016 Elsevier Inc. All rights reserved.
引用
收藏
页码:206 / 213
页数:8
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