Study of gold nanorods–protein interaction by localized surface plasmon resonance spectroscopy

In this paper, gold nanorods’ (GNRs) interaction with different proteins (i.e. carbonic anhydrase, lysozyme, ovalbumin and bovine serum albumin (BSA)) at physiological pH is investigated using localized surface plasmon resonance (LSPR) spectroscopy. We observe that the incubation of these proteins at different concentrations with cetyltrimethylammonium bromide-capped GNRs of three aspect ratios induces dramatic changes in the extinction spectra of the nanoparticles. In particular, we correlate the position and shape of the longitudinal LSPR peaks to the ability of the proteins to specifically interact with GNRs’ surface. The different types of behaviour observed are explained by the exposed molecular surface area of the proteins’ cysteine residues as modelled on the basis of their respective X-ray crystallographic data structures. Cysteine is the only amino acid that exhibits an SH group that is well known to have a strong affinity to gold. The presence and the accessibility of such a residue may explain the protein binding to GNRs. The isoelectric point of the proteins is also an important characteristic to take into account, as the electrostatic strength between GNRs and protein explains some of the cases where aggregates are formed.

[1]  Nathalie Lidgi-Guigui,et al.  Localized Surface Plasmon Resonance (LSPR) Biosensor for the Protein Detection , 2012, Plasmonics.

[2]  Rebekah A. Drezek,et al.  Tunable Nanostructures as Photothermal Theranostic Agents , 2011, Annals of Biomedical Engineering.

[3]  Dakrong Pissuwan,et al.  Targeted destruction of murine macrophage cells with bioconjugated gold nanorods , 2007 .

[4]  L. Chau,et al.  Sensing capability of the localized surface plasmon resonance of gold nanorods. , 2007, Biosensors & bioelectronics.

[5]  Younan Xia,et al.  Gold nanostructures: engineering their plasmonic properties for biomedical applications. , 2006, Chemical Society reviews.

[6]  Xiaohua Huang,et al.  Gold Nanorods: From Synthesis and Properties to Biological and Biomedical Applications , 2009, Advanced materials.

[7]  R. Palmer,et al.  Weak precursor state binding of protein molecules to size-selected gold nanoclusters on surfaces , 2008 .

[8]  W. D. Geoghegan,et al.  Adsorption of horseradish peroxidase, ovomucoid and anti-immunoglobulin to colloidal gold for the indirect detection of concanavalin A, wheat germ agglutinin and goat anti-human immunoglobulin G on cell surfaces at the electron microscopic level: a new method, theory and application. , 1977, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[9]  Xiaohua Huang,et al.  Surface plasmon resonance scattering and absorption of anti-EGFR antibody conjugated gold nanoparticles in cancer diagnostics: applications in oral cancer. , 2005, Nano letters.

[10]  S. Curry,et al.  Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. , 2000, Journal of molecular biology.

[11]  Yu Zhang,et al.  Gold nanocages covered with thermally-responsive polymers for controlled release by high-intensity focused ultrasound. , 2011, Nanoscale.

[12]  R Diamond,et al.  Real-space refinement of the structure of hen egg-white lysozyme. , 1977, Journal of molecular biology.

[13]  Kadir Aslan,et al.  Plasmon light scattering in biology and medicine: new sensing approaches, visions and perspectives. , 2005, Current opinion in chemical biology.

[14]  Kort Travis,et al.  Plasmon resonance coupling of metal nanoparticles for molecular imaging of carcinogenesis in vivo. , 2007, Journal of biomedical optics.

[15]  Hui Zhang,et al.  Gold nanocages: bioconjugation and their potential use as optical imaging contrast agents. , 2005, Nano letters.

[16]  Xiaohua Huang,et al.  Cancer cell imaging and photothermal therapy in the near-infrared region by using gold nanorods. , 2006, Journal of the American Chemical Society.

[17]  P. Prasad,et al.  Preparation of Gold Nanoparticles and their Applications in Anisotropic Nanoparticle Synthesis and Bioimaging , 2009 .

[18]  Anurag Sharma,et al.  Effect of the sugar and polyol additives on the aggregation kinetics of BSA in the presence of N-cetyl-N,N,N-trimethyl ammonium bromide. , 2010, Journal of colloid and interface science.

[19]  Younan Xia,et al.  Gold and silver nanoparticles: a class of chromophores with colors tunable in the range from 400 to 750 nm. , 2003, The Analyst.

[20]  A G Leslie,et al.  Crystal structure of uncleaved ovalbumin at 1.95 A resolution. , 1991, Journal of molecular biology.

[21]  William G. Hardin,et al.  Conjugation of antibodies to gold nanorods through Fc portion: synthesis and molecular specific imaging. , 2013, Bioconjugate chemistry.

[22]  A Paul Alivisatos,et al.  A nanoplasmonic molecular ruler for measuring nuclease activity and DNA footprinting , 2006, Nature nanotechnology.

[23]  Q. Huo,et al.  Dynamic light scattering for gold nanorod size characterization and study of nanorod–protein interactions , 2012, Gold Bulletin.

[24]  C. D. Geddes,et al.  Reviews in Plasmonics 2010 , 2012, Reviews in Plasmonics.

[25]  L. J. Harris,et al.  Refined structure of an intact IgG2a monoclonal antibody. , 1997, Biochemistry.

[26]  Werner Braun,et al.  Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules , 1998, J. Comput. Chem..

[27]  T A Jones,et al.  Refined structure of human carbonic anhydrase II at 2.0 Å resolution , 1988, Proteins.

[28]  F M Richards,et al.  Areas, volumes, packing and protein structure. , 1977, Annual review of biophysics and bioengineering.

[29]  J. Heath,et al.  Residue-specific immobilization of protein molecules by size-selected clusters , 2005, Journal of The Royal Society Interface.