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Research Results from Florida State University Update Understanding of Peptides and Proteins (Understanding the self-assembly of proteins onto gold...

September 9, 2014



Research Results from Florida State University Update Understanding of Peptides and Proteins (Understanding the self-assembly of proteins onto gold nanoparticles and quantum dots driven by metal-histidine coordination)

By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Peptides and Proteins. According to news reporting originating from Tallahassee, Florida, by NewsRx correspondents, research stated, "Coupling of polyhistidine-appended biomolecules to inorganic nanocrystals driven by metal-affinity interactions is a greatly promising strategy to form hybrid bioconjugates. It is simple to implement and can take advantage of the fact that polyhistidine-appended proteins and peptides are routinely prepared using well established molecular engineering techniques."

Our news editors obtained a quote from the research from Florida State University, "A few groups have shown its effectiveness for coupling proteins onto Zn-or Cd-rich semiconductor quantum dots (QDs). Expanding this conjugation scheme to other metal-rich nanoparticles (NPs) such as AuNPs would be of great interest to researchers actively seeking effective means for interfacing nanostructured materials with biology. In this report, we investigated the metal-affinity driven self-assembly between AuNPs and two engineered proteins, a His7-appended maltose binding protein (MBP-His) and a fluorescent His6-terminated mCherry protein. In particular, we investigated the influence of the capping ligand affinity to the nanoparticle surface, its density, and its lateral extension on the AuNP-protein self-assembly. Affinity gel chromatography was used to test the AuNP-MPB-His7 self-assembly, while NP-to-mCherry-His6 binding was evaluated using fluorescence measurements. We also assessed the kinetics of the self-assembly between AuNPs and proteins in solution, using time-dependent changes in the energy transfer quenching of mCherry fluorescent proteins as they immobilize onto the AuNP surface. This allowed determination of the dissociation rate constant, Kd(-1) ? 1-5 nM."

According to the news editors, the research concluded: "Furthermore, a close comparison of the protein self-assembly onto AuNPs or QDs provided additional insights into which parameters control the interactions between imidazoles and metal ions in these systems."

For more information on this research see: Understanding the self-assembly of proteins onto gold nanoparticles and quantum dots driven by metal-histidine coordination. Acs Nano, 2013;7(11):10197-210. (American Chemical Society - www.acs.org; Acs Nano - www.pubs.acs.org/journal/ancac3)

The news editors report that additional information may be obtained by contacting F. Aldeek, Dept. of Chemistry and Biochemistry, Florida State University , 95 Chieftan Way, Tallahassee, Florida 32306, United States. Additional authors for this research include M. Safi, N. Zhan, G. Palui and H. Mattoussi (see also Peptides and Proteins).

Keywords for this news article include: Tallahassee, Florida, United States, North and Central America, Amino Acids, Emerging Technologies, Gold Nanoparticles, Nanotechnology, Peptides, Peptides and Proteins, Proteins, Quantum Dots, Quantum Physics.

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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