By a News Reporter-Staff News Editor at Science Letter -- New research on Proteins is the subject of a report. According to news reporting originating in Amman, Jordan, by NewsRx journalists, research stated, "Investigating the adsorption process of proteins on nanoparticle surfaces is essential to understand how to control the biological interactions of functionalized nanoparticles. In this work, a library of spherical and rod-shaped gold nanoparticles (GNPs) was used to evaluate the process of protein adsorption to their surfaces."
The news reporters obtained a quote from the research from the University of Jordan, "The binding of a model protein (bovine serum albumin, BSA) to GNPs as a function of particle shape, size, and surface charge was investigated. Two independent comparative analytical methods were used to evaluate the adsorption process: steady-state fluorescence quenching titration and affinity capillary electrophoresis (ACE). Although under favorable electrostatic conditions kinetic analysis showed a faster adsorption of BSA to the surface of cationic GNPs, equilibrium binding constant determinations indicated that BSA has a comparable binding affinity to all of the GNPs tested, regardless of surface charge. BSA was even found to adsorb strongly to GNPs with a pegylated/neutral surface. However, these fluorescence titrations suffer from significant interference from the strong light absorption of the GNPs. The BSA-GNP equilibrium binding constants, as determined by the ACE method, were 10(5) times lower than values determined using spectroscopic titrations. While both analytical methods could be suitable to determine the binding constants for protein adsorption to NP surfaces, both methods have limitations that complicate the determination of protein-GNP binding constants. The optical properties of GNPs interfere with K-a determinations by static fluorescence quenching analysis. ACE, in contrast, suffers from material compatibility issues, as positively charged GNPs adhere to the walls of the capillary during analysis."
According to the news reporters, the research concluded: "Researchers seeking to determine equilibrium binding constants for protein-GNP interactions should therefore utilize as many orthogonal techniques as possible to study a protein-GNP system."
For more information on this research see: Nanoparticle-Protein Interactions: A Thermodynamic and Kinetic Study of the Adsorption of Bovine Serum Albumin to Gold Nanoparticle Surfaces. Langmuir, 2013;29(48):14984-14996. Langmuir can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Langmuir - www.pubs.acs.org/journal/langd5)
Our news correspondents report that additional information may be obtained by contacting S.P. Boulos, University of Jordan, Fac Pharm, Dept. of Pharmaceut & Pharmaceut Technol, Amman 11942, Jordan. Additional authors for this research include T.A. Davis, J.A. Yang, S.E. Lohse, A.M. Alkilany, L.A. Holland and C.J. Murphy (see also Proteins).
Keywords for this news article include: Asia, Amman, Jordan, Blood Proteins, Nanotechnology, Gold Nanoparticles, Acute-Phase Proteins, Bovine Serum Albumin, Emerging Technologies
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