Reports Summarize Proteomics Study Results from Argonne National Laboratory (Peptide-Modified Dendrimers as Templates for the Production of Highly Reactive Catalytic Nanomaterials)
By a News Reporter-Staff News Editor at Life Science Weekly -- New research on Proteomics is the subject of a report. According to news reporting originating from Argonne, Illinois, by NewsRx correspondents, research stated, "Peptide-driven nanomaterials synthesis and assembly has become a significant research thrust due to the capability to generate a range of multifunctional materials with high spatial precision and tunable properties. Despite the extensive amount of available literature, the majority of studies report the use of free peptides to drive synthesis and assembly."
Our news editors obtained a quote from the research from Argonne National Laboratory, "Such strategies are not an entirely accurate representation of nature, as many materials binding peptides found in biological systems are sterically constrained to a larger biological motif. Herein we report the synthesis of catalytic Pd nanomaterials using constrained peptides covalently attached to the surface of small, water-soluble dendrimers. Using the R5 peptide conjugated to polyamidoamine dendrimer as a bioconjugate, Pd nanomaterials were generated that displayed altered morphologies compared to nanomaterials templated with free R5. It was discovered that the peptide surface density on the dendrimer affected the resulting nanoscale morphology. Furthermore, the catalytic activities of Pd materials templated with R5/dendrimer are higher as compared to the R5-templated Pd materials for the hydrogenation of ally] alcohol, with an average increase in turnover frequency of similar to 1500 mol product (mol Pd X h)(-1). Small angle X-ray scattering analysis and dynamic light scattering indicate that Pd derived from R5/dendrimer templates remained less aggregated in solution and displayed more available reactive Pd surface area. Such morphological changes in solution are attributed to the constrained peptide binding motifs, which altered the Pd morphology and subsequent properties."
According to the news editors, the research concluded: "Moreover, the results of this study suggest that constrained materials binding peptide systems can be employed as a means to alter morphology and improve resulting properties."
For more information on this research see: Peptide-Modified Dendrimers as Templates for the Production of Highly Reactive Catalytic Nanomaterials. Chemistry of Materials, 2014;26(14):4082-4091. Chemistry of Materials can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Chemistry of Materials - www.pubs.acs.org/journal/cmatex)
The news editors report that additional information may be obtained by contacting N.M. Bedford, Argonne Natl Lab, Xray Sci Div, Argonne, IL 60439, United States. Additional authors for this research include R. Bhandari, J.M. Slocik, S. Seifert, R.R. Naik and M.R. Knecht (see also Proteomics).
Keywords for this news article include: Argonne, Illinois, Peptides, Proteins, Proteomics, Nanomaterial, United States, Nanotechnology, Emerging Technologies, North and Central America
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