Characterisation of the de-agglomeration effects of bovine serum albumin on nanoparticles in aqueous suspension

Colloids and Surfaces B: Biointerfaces

Volumn 75, Issue 1, 2010, Pages 275-281

  Tantra, Ratna ^a   Tompkins, Jordan ^a   Quincey, Paul ^a  

^a NATIONAL PHYSICAL LABORATORY   (United Kingdom)

Author keywords

Albumin; De agglomeration; Nanoparticles; Stability; Titanium dioxide; Zinc oxide

Indexed keywords

ADSORPTION KINETICS; AGGLOMERATION EFFECTS; ALBUMIN; AQUEOUS MEDIA; AQUEOUS SUSPENSIONS; BOVINE SERUM ALBUMINS; CERTAIN FACTOR; CHARACTERISATION; DE-AGGLOMERATION; ELECTROSTATIC REPULSION; ENHANCED STABILITY; SUBMICRON; TIO; ZETA POTENTIAL MEASUREMENTS; ZNO;

ADSORPTION; AGGLOMERATION; NANOPARTICLES; SCANNING ELECTRON MICROSCOPY; SEMICONDUCTING ZINC COMPOUNDS; STABILITY; SUSPENSIONS (FLUIDS); TITANIUM; TITANIUM DIOXIDE; TITANIUM OXIDES; ZINC; ZINC OXIDE;

BODY FLUIDS;

BOVINE SERUM ALBUMIN; NANOPARTICLE; TITANIUM DIOXIDE; ZINC OXIDE;

ADSORPTION; AQUEOUS SOLUTION; ARTICLE; CONTROLLED STUDY; MOLECULAR STABILITY; PARTICLE SIZE; PRIORITY JOURNAL; STEREOSPECIFICITY; ZETA POTENTIAL;

ANIMALS; CATTLE; LATEX; MICROSPHERES; NANOPARTICLES; PARTICLE SIZE; POLYLYSINE; SERUM ALBUMIN, BOVINE; SUSPENSIONS; TITANIUM; WATER; ZINC OXIDE;

BOVINAE;

EID: 70449651738     PISSN: 09277765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2009.08.049     Document Type: Article

References (21)

1. Saltiel C., and Giesche H. Needs and opportunities for nanoparticle characterization. J. Nanoparticle Res. 2 (2000) 325-326
2. Jiang J.K., Oberdorster G., and Biswas P. Characterization of size, surface charge, and agglomeration state of nanoparticle dispersions for toxicological studies. J. Nanoparticle Res. 11 1 (2009) 77-89
3. Richter V., Potthoff A., Pompe W., Gelinsky M., Ikonomidou H., Bastian S., Schirmer K., Scholz S., and Hofinger J. Evaluation of health risks of nano- and microparticles. Powder metallurgy 51 1 (2008) 8-9
4. Bihari P., Vippola M., Schultes S., Praetner M., Khandoga A.G., Reichel C.A., Coester C., Tuomi T., Rehberg M., and Krombach F. Optimized dispersion of nanoparticles for biological in vitro and in vivo studies. Particle Fiber Toxicol. 5 (2008) 14
5. Zhang M.Q., Desai T., and Ferrari M. Proteins and cells on PEG immobilized silicon surfaces. Biomaterials 19 10 (1998) 953-960
6. Zunszain P.A., Ghuman J., Komatsu T., Tsuchida E., and Curry S. Crystal structural analysis of human serum albumin complexed with hemin and fatty acid. BMC Struct. Biol. 7 3 (2003) 6
7. Powers K.W., Brown S.C., Krishna V.B., Wasdo S.C., Moudgil B.M., and Roberts S.M. Research strategies for safety evaluation of nanomaterials. Part VI. Characterization of nanoscale particles for toxicological evaluation. Toxicol. Sci. 90 2 (2006) 296-303
8. Koh A.L., Shachaf C.M., Elchuri S., Nolan G.P., and Sinclair R. Electron microscopy localization and characterization of functionalized composite organic-inorganic SERS nanoparticles on leukemia cells. Ultramicroscopy 109 1 (2008) 111-121
9. Wang C.M., Baer D.R., Amonette J.E., Engelhard M.H., Antony J.J., and Qiang Y. Electron beam-induced thickening of the protective oxide layer around Fe nanoparticles. Ultramicroscopy 108 1 (2007) 43-51
10. Rahman I.A., Vejayakumaran P., Sipaut C.S., Ismail J., and Chee C.K. Effect of the drying techniques on the morphology of silica nanoparticles synthesized via sol-gel process. Ceram. Int. 34 8 (2008) 2059-2066
11. Gonzalez S., Fernandez-Lorente M., and Gilaberte-Calzada Y. The latest on skin photoprotection. Clin. Dermatol. 26 6 (2008) 614-626
12. Pohl M., Hogekamp S., Hoffmann N.Q., and Schuchmann H.P. Dispersion and deagglomeration of nanoparticles with ultrasound. Chem. Eng. Technol. 76 4 (2004) 392-396
13. Tantra R., Brown R.J.C., Milton M.J.T., and Gohil D. A practical method to fabricate gold substrates for surface-enhanced Raman spectroscopy. Appl. Spectrosc. 62 9 (2008) 992-1000
14. Schulze C., Kroll A., Lehr C.-M., Schfer U., Becker F., Schnekenburger K., Isfort J.C.S., Landsiedel R., and Wohlleben W. Not ready to use-overcoming pitfalls when dispersing nanoparticles in physiological media. Nanotoxicology 2 2 (2008) 51-61
15. Hunter R.J. Foundations of Colloid Science. 2nd ed. (2001), Clarendon Press, Oxford
16. Sato K., Li J.G., Kamiya H., and Ishigaki T. Ultrasonic dispersion of TiO2 nanoparticles in aqueous suspension. J. Am. Ceram. Soc. 91 8 (2008) 2481-2487
17. Min Y.J., Akbulut M., Kristiansen K., Golan Y., and Israelachvili J. The role of interparticle and external forces in nanoparticle assembly. Nat. Mater. 7 7 (2008) 527-538
18. In: Tadros T.F. (Ed). Colloid Stability: The Role of Surface Forces-Part I vol. 1 (2006), Wiley
19. Cedervall T., Lynch I., Lindman S., Berggard T., Thulin E., Nilsson H., Dawson K.A., and Linse S. Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc. Natl. Acad. Sci. U.S.A. 104 7 (2007) 2050-2055
20. Sahoo B., Goswami M., Nag S., and Maiti S. Spontaneous formation of a protein corona prevents the loss of quantum dot fluorescence in physiological buffers. Chem. Phys. Lett. 445 4-6 (2007) 217-220
21. Lundqvist M., Stigler J., Elia G., Lynch I., Cedervall T., and Dawson K.A. Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc. Natl. Acad. Sci. U.S.A. 105 38 (2008) 14265-14270