Peptide nanowires for coordination and signal transduction of peroxidase biosensors to carbon nanotube electrode arrays

被引:16
作者
Yeh, J. I.
Lazareck, A.
Kim, J. Ho
Xu, J.
Du, S.
机构
[1] Univ Pittsburgh, Sch Med, Dept Biol Struct, Pittsburgh, PA 15260 USA
[2] Univ Pittsburgh, Dept Bioengn, Pittsburgh, PA 15260 USA
[3] Brown Univ, Div Engn, Providence, RI 02912 USA
关键词
peptide nanowire; carbon nanotube electrode; NADH peroxidase; gold nanoparticle; metallized peptide; nanoarrays;
D O I
10.1016/j.bios.2007.06.019
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
strategy of metallizing peptides to serve as conduits of electronic signals that bridge between a redox enzyme and a carbon-nanotube electrode has been developed with enhanced results. In conjunction, a protocol to link the biological elements to the tips of carbon nanotubes has been developed to optimize contact and geometry between the redox enzyme and the carbon nanotube electrode array. A peptide nanowire of 33 amino acids, comprised of a leucine zipper motif, was mutated to bind divalent metals, conferring conductivity into the peptide. Reaction between a thiolate of the peptide with the sulfenic acid of the NADH peroxidase enzyme formed a peptide-enzyme assembly that are fully primed to transduce electrons out of the enzyme active site to an electrode. Scanning electron microscopy shows immobilization and linking of the assembly specifically to the tips of carbon nanotube electrodes, as designed. Isothermal titration calorimetry and mass spectrometry indicate a binding stoichiometry of at least three metals bound per peptide strand. Overall, these results highlight the gain that can be achieved when the signal tranducing units of a biosensor are aligned through directed peptide chemistry. (c) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码:568 / 574
页数:7
相关论文
共 47 条
[1]   Organization of 'nanocrystal molecules' using DNA [J].
Alivisatos, AP ;
Johnsson, KP ;
Peng, XG ;
Wilson, TE ;
Loweth, CJ ;
Bruchez, MP ;
Schultz, PG .
NATURE, 1996, 382 (6592) :609-611
[2]   Recent developments in dynamic electrochemical studies of adsorbed enzymes and their active sites [J].
Armstrong, FA .
CURRENT OPINION IN CHEMICAL BIOLOGY, 2005, 9 (02) :110-117
[3]  
Claiborne A, 2001, ADV PROTEIN CHEM, V58, P215
[4]   Protein-sulfenic acids: Diverse roles for an unlikely player in enzyme catalysis and redox regulation [J].
Claiborne, A ;
Yeh, JI ;
Mallett, TC ;
Luba, J ;
Crane, EJ ;
Charrier, V ;
Parsonage, D .
BIOCHEMISTRY, 1999, 38 (47) :15407-15416
[5]   DNA monolayer on gold substrates characterized by nanoparticle labeling and scanning force microscopy [J].
Csáki, A ;
Möller, R ;
Straube, W ;
Köhler, JM ;
Fritzsche, W .
NUCLEIC ACIDS RESEARCH, 2001, 29 (16) :art. no.-e81
[6]   A parallel approach for subwavelength molecular surgery using gene-specific positioned metal nanoparticles as laser light antennas [J].
Csaki, Andrea ;
Garwe, Frank ;
Steinbruck, Andrea ;
Maubach, Gunter ;
Festag, Grit ;
Weise, Anja ;
Riemann, Iris ;
Koenig, Karsten ;
Fritzsche, Wolfgang .
NANO LETTERS, 2007, 7 (02) :247-253
[7]  
Dresselhaus MS, 2001, CARBON NANOTUBES SYN
[8]   Electrochemical DNA sensors [J].
Drummond, TG ;
Hill, MG ;
Barton, JK .
NATURE BIOTECHNOLOGY, 2003, 21 (10) :1192-1199
[9]   A microRNA biosensor based on direct chemical ligation and electrochemically amplified detection [J].
Gao, Zhiqiang ;
Yu, Yuan Hong .
SENSORS AND ACTUATORS B-CHEMICAL, 2007, 121 (02) :552-559
[10]   Quantitative measurements and modeling of kinetics in nucleic acid monolayer films using SPR spectroscopy [J].
Georgiadis, R ;
Peterlinz, KP ;
Peterson, AW .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2000, 122 (13) :3166-3173