Functionalized Carbon Nanotubes for Detecting Viral Proteins

William Penn University, Filadelfia, Pennsylvania, United States
Nano Letters (Impact Factor: 13.59). 11/2007; 7(10):3086-91. DOI: 10.1021/nl071572l
Source: PubMed

ABSTRACT We investigated the biocompatibility, specificity, and activity of a ligand-receptor-protein system covalently bound to oxidized single-walled carbon nanotubes (SWNTs) as a model proof-of-concept for employing such SWNTs as biosensors. SWNTs were functionalized under ambient conditions with either the Knob protein domain from adenovirus serotype 12 (Ad 12 Knob) or its human cellular receptor, the CAR protein, via diimide-activated amidation. We confirmed the biological activity of Knob protein immobilized on the nanotube surfaces by using its labeled conjugate antibody and evaluated the activity and specificity of bound CAR on SWNTs, first, in the presence of fluorescently labeled Knob, which interacts specifically with CAR, and second, with a negative control protein, YieF, which is not recognized by biologically active CAR proteins. In addition, current-gate voltage (I-V(g)) measurements on a dozen nanotube devices explored the effect of protein binding on the intrinsic electronic properties of the SWNTs, and also demonstrated the devices' high sensitivity in detecting protein activity. All data showed that both Knob and CAR immobilized on SWNT surfaces fully retained their biological activities, suggesting that SWNT-CAR complexes can serve as biosensors for detecting environmental adenoviruses.

Download full-text


Available from: a t charlie Johnson, Jul 22, 2014
  • Source
    • "The molecular mechanism by which atomic interactions at the surface of the carbon nanotube influence the mobility of carriers within the carbon lattice is a subject of great current interest [78] directly relevant to understanding the mode of odorant sensing by DNA-coated nanotubes [79]. All-atom molecular dynamics studies of DNA-carbon nanotube interactions show that a pi-pi stacking interaction between the DNA bases and the nanotube sidewall guides the DNA-nanotube interaction [34], which is sufficiently strong [80] to allow sensing functions to occur in aqueous solution [81]. Specific dominant conformations have been identified through the use of replica exchange molecular dynamics (REMD) [82] . "
    [Show abstract] [Hide abstract]
    ABSTRACT: The analysis of breath and body odors can provide valuable information relevant to disease detection, diagnosis and treatment. A variety of technical developments are being pursued to develop electronic devices intended to analyze volatile components of breath and body odors with the sensitivity, selectivity, and learning ability of high-end mammalian olfactory systems. Here, we describe a new sensor technology that has the potential to supply a large set of diverse and sensitive odorant sensors with electronic readout to provide information-rich odorant-elicited signals for analysis by pattern recognition algorithms. In addition, we demonstrate that these sensors can provide discrimination of odorant homologues consisting of aldehydes and organic acids commonly found in human breath and other body emanations over a range of concentrations.
    IEEE Sensors Journal 02/2010; 10(1-10):159 - 166. DOI:10.1109/JSEN.2009.2035670 · 1.85 Impact Factor
  • Source
    • "Since the discovery of carbon nanotubes (CNTs) in 1991 [1], CNTs have raised considerable attention due to their fascinating structures and properties (electronic, optical, thermal, mechanical etc.) [2] [3]. Recently, its potential application in biotechnology has attracted much interest, as CNTs have been reported to exhibit great advantages in biosensors [4] [5], biomedical devices [6] and drug delivery systems (DDS) [7] [8] etc. Pristine CNTs are highly hydrophobic, so the main obstacle in the utilization of CNTs in biological and medicinal chemistry is their poor solubility in aqueous-based biological milieu. Biomolecule functionalization is one option to overcome such defects. "
    [Show abstract] [Hide abstract]
    ABSTRACT: Non-covalent adsorption of proteins onto carbon nanotubes is important to understand the environmental and biological activity of carbon nanotubes as well as their potential applications in nanostructure fabrication. In this study, the adsorption dynamics and features of a model protein (the A sub-domain of human serum albumin) onto the surfaces of carbon nanotubes with different diameters were investigated out by molecular dynamics simulation. The adsorption behaviors were observed by both trajectory and quantitative analyses. During the adsorption process, the secondary structures of alpha-helices in the model protein were slightly affected. However, the random coils connecting these alpha-helices were strongly affected and this made the tertiary structure of protein change. The conformation and orientation selection of the protein were induced by the properties and the texture of surfaces indicated by the interaction curve. In addition, the stepwise adsorption dynamics of these processes are found. The mechanism of induced stepwise conformational change of protein on carbon nanotube surfaces would be helpful to better understand the protein-surface interaction at the molecular level.
    Biomaterials 08/2008; 29(28):3847-55. DOI:10.1016/j.biomaterials.2008.06.013 · 8.31 Impact Factor
  • Source
    • "Another approach may be to use insights into the mechanism of viral formation to develop chemical approaches to inhibit the synthesis process. In addition, work in this area may lead to novel biomedical devices, such as highly sensitive real-time virus protein detectors [6]. From the point of view of materials science and engineering, viruses and virus-inspired structures could be utilized as specific and structurally robust self-replicating nanoscale 'packages' or 'carriers', for example. "
    [Show abstract] [Hide abstract]
    ABSTRACT: The prospect of understanding and controlling the structure, formation and properties of nanoscale virus capsids has challenged researchers from disciplines as diverse as biology, chemistry, mechanical engineering and physics for over half a century. In this review, I will describe a number of theoretical approaches to this. The most well-known approach is that of Caspar and Klug, developed in the 1950's and 60's, and I will outline both the original idea and recent extensions of it. I will then focus on an alternative approach developed by Nelson et al. that combines notions from crystallography and continuum mechanics, detailing the main ideas and further developments based on these. I will also touch on key AFM nanoindentation experiments of viral capsids, exploring how they can be understood within Nelson et al.'s theoretical framework.
Show more