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Researchers at Mississippi State University Release New Data on Gold Nanoparticles

May 27, 2014



By a News Reporter-Staff News Editor at Life Science Weekly -- Data detailed on Gold Nanoparticles have been presented. According to news reporting out of Mississippi State, Mississippi, by NewsRx editors, research stated, "Gold nanoparticles (AuNPs) are an attractive delivery vector in biomedicine because of their low toxicity and unique electronic and chemical properties. AuNP bioconjugates can be used in many applications, including nanomaterials, biosensing, and drug delivery."

Our news journalists obtained a quote from the research from Mississippi State University, "While the phenomenon of spontaneous protein-AuNP adsorption is well-known, the structural and mechanistic details of this interaction remain poorly understood. As a result, predicting the orientation and structure of proteins on the nanoparticle surface remains a challenge. New techniques are therefore needed to characterize the structural properties of proteins as they bind to AuNPs. We have developed a straightforward and rapid NMR-based approach to quantitatively characterize the protein-AuNP interaction. This approach is immune to the inner filter effect, which complicates fluorescence measurements, and it can be performed without prior centrifugation of samples. Using a data set of six proteins, ranging in size from 3 to 583 residues, we measured the stoichiometry of binding to AuNPs with a diameter of 15 nm. The stoichiometry of binding can be predicted based on simple geometric considerations assuming that proteins remain globular on the AuNP surface. Using our approach, we find that a protein lacking cysteine residues can be displaced from AuNPs using a small organothiol compound, but proteins with surface cysteines are resistant to displacement."

According to the news editors, the research concluded: "From this data we develop a model for adsorption consisting of three steps: an initial reversible association step, a rearrangement/reorientation step on the AuNP surface, and a final cysteine-dependent 'hardening' step, after which binding becomes irreversible."

For more information on this research see: A Three-Step Model for Protein-Gold Nanoparticle Adsorption. Journal of Physical Chemistry C, 2014;118(15):8134-8142. Journal of Physical Chemistry C can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Journal of Physical Chemistry C - www.pubs.acs.org/journal/jpccck)

Our news journalists report that additional information may be obtained by contacting A.L. Wang, Mississippi State University, Dept. of Chem, Mississippi State, MS 39762, United States. Additional authors for this research include K. Vangala, T. Vo, D.M. Zhang and N.C. Fitzkee (see also Gold Nanoparticles).

Keywords for this news article include: Peptides, Proteins, Amino Acids, United States, Nanotechnology, Mississippi State, Gold Nanoparticles, Emerging Technologies, North and Central America

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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