文献类型：期刊文献

英文题名：Peptide-Induced Affinity Binding of Carbonic Anhydrase to Carbon Nanotubes

作者：Chen, Xiaoxing[1];Wang, Yibing[1];Wang, Ping[1]

机构：[1]E China Univ Sci & Technol, Sch Biotechnol, Biomed Nanotechnol Ctr, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2015

卷号：31

期号：1

起止页码：397

外文期刊名：LANGMUIR

收录：;EI(收录号：20150400445827);WOS:【SCI-EXPANDED(收录号:WOS:000348085900050)】；

基金：This work was supported by the National Natural Science Foundation of China (21303050 and 31471659), the China Postdoctoral Science Foundation (2013M540334), and the Engagement Fund of Interdisciplinary and Major Project of the Ministry of National Education (wk0913002).

语种：英文

外文关键词：Biochemistry - Enzyme activity - Hybrid materials - Single-walled carbon nanotubes (SWCN) - Surface chemistry - Peptides - Yarn - Carbonic anhydrase - Catalyst activity

摘要：Although affinity binding between short chain peptides and carbon nanotube (CNT) has been reported, little is known for the study of proteins with CNT recognition and specific binding capabilities. Herein, carbonic anhydrase (CA) was functionalized via protein fusion with a single-walled carbon nanotube (SWNTs)-binding peptide, thereby forming a bioactive protein with high affinity binding capability. TEM and AFM analyses showed that the fusion CA could firmly coat to SWNTs with a surface coverage over 51%, while the enzyme maintained its catalytic activity. Structural analysis revealed that slight conformation changes were induced as a result of the fusion; however, the affinity binding of CA to the hydrophobic surface of SWNTs restored the native structure of the protein, with the conformation of the SWNT-bound CA largely resembling that of the native parent enzyme. Interfacial interactions between the fusion CA and SWNT were further investigated with Raman spectrometry and microscopic analysis. The results suggested that such peptide-induced CNT-protein binding allows the development of bioactive hybrid materials with the native structures of the protein moieties largely undisrupted.