Florida State University Target Peptides and Proteins -->
By a News Reporter-Staff News Editor at Life Science Weekly -- Fresh data on Peptides and Proteins are presented in a new report. According to news reporting originating in Tallahassee, Florida, by NewsRx journalists, 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."
The news reporters 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 His(7)-appended maltose binding protein (MBP-His) and a fluorescent His(6)-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-His(7) self-assembly, while NP-to-mCherry-His(6) 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, K-d(-1) similar to 1-5 nM."
According to the news reporters, 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):10197-10210. ACS Nano can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; ACS Nano - www.pubs.acs.org/journal/ancac3)
Our news correspondents report that additional information may be obtained by contacting F. Aldeek, Florida State University, Dept. of Chem & Biochem, Tallahassee, FL 32306, United States. Additional authors for this research include M. Safi, N.Q. Zhan, G. Palui and H. Mattoussi (see also Peptides and Proteins).
Keywords for this news article include: Florida, Histidine, Tallahassee, Quantum Dots, United States, Nanotechnology, Quantum Physics, Cyclic Amino Acids, Gold Nanoparticles, Emerging Technologies, Essential Amino Acids, Peptides and Proteins, North and Central America
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