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Researchers from University of Oslo Provide Details of New Studies and Findings in the Area of Protein Nanoparticles

May 30, 2014

By a News Reporter-Staff News Editor at Science Letter -- Data detailed on Protein Nanoparticles have been presented. According to news reporting originating from Oslo, Norway, by NewsRx correspondents, research stated, "We investigate the role of different mesoscopic interactions (Coulomb, charge regulation, and ion-dipole 'surface patch' effects) on the binding of bovine serum albumin (BSA) and beta-lactoglobulin (BLG) to a cationic gold nanoparticle (TTMA+)."

Our news editors obtained a quote from the research from the University of Oslo, "The results demonstrate that the charge-regulation mechanism plays a vital role for selectivity of protein-nanoparticle complexation at low salt concentration. At slightly higher ionic strengths, charge-dipole effects are the dominating driving force."

According to the news editors, the research concluded: "Thus, very small variations in salt concentration strongly influence the origin of complexation."

For more information on this research see: Effect of Charge Regulation and Ion-Dipole Interactions on the Selectivity of Protein-Nanoparticle Binding. Langmuir, 2014;30(14):4078-4083. Langmuir can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society -; Langmuir -

The news editors report that additional information may be obtained by contacting F.L.B. da Silva, University of Oslo, Dept. of Phys, NO-0316 Oslo, Norway. Additional authors for this research include M. Bostrom and C. Persson (see also Protein Nanoparticles).

Keywords for this news article include: Oslo, Norway, Europe, Nanotechnology, Emerging Technologies, Protein Nanoparticles

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Source: Science Letter

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