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Study Data from University of Padova Update Understanding of Proteomics (Reversible chirality control in peptide-functionalized gold nanoparticles)

September 9, 2014

By a News Reporter-Staff News Editor at Life Science Weekly -- Data detailed on Proteomics have been presented. According to news reporting originating from Padova, Italy, by NewsRx correspondents, research stated, "We report the induction of chiroptical properties in 2 nm diameter gold nanoparticles passivated with short peptides characterized by the Aib-l-Ala repetition in their sequence. The nanoparticles present relevant ECD signals in the 300-650 nm wavelength region, corresponding to the gold nanoparticle's quantized electronic structure."

Our news editors obtained a quote from the research from the University of Padova, "Although the only chiral amino acid present in the peptide sequences is l-Ala, the particles show mirror image spectra like those of enantiomers according to the number of amino acids in the main chain (odd or even). Such a behavior appears to be strongly influenced by the secondary structure assumed by the peptides when passivating the nanoparticles and vanishes when the sequence is long enough to assume a 310-helix conformation."

According to the news editors, the research concluded: "Moreover, chirality control is a reversible process and can be deactivated or reactivated by increasing or decreasing the temperature."

For more information on this research see: Reversible chirality control in peptide-functionalized gold nanoparticles. Acs Nano, 2013;7(11):9933-9. (American Chemical Society -; Acs Nano -

The news editors report that additional information may be obtained by contacting E. Longo, Dept. of Chemical Sciences, University of Padova , Via Marzolo 1, 35131 Padova, Italy. Additional authors for this research include A. Orlandin, F. Mancin, P. Scrimin and A. Moretto (see also Proteomics).

Keywords for this news article include: Padova, Italy, Europe, Emerging Technologies, Gold Nanoparticles, Nanotechnology, Peptides, Proteins, Proteomics.

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Source: Life Science Weekly

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