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New Findings from Northwestern University Describe Advances in Proteomics (Tuning nanostructure dimensions with supramolecular twisting)

July 8, 2014

By a News Reporter-Staff News Editor at Life Science Weekly -- A new study on Proteomics is now available. According to news reporting originating in Evanston, Illinois, by NewsRx journalists, research stated, "Peptide amphiphiles are molecules containing a peptide segment covalently bonded to a hydrophobic tail and are known to self-assemble in water into supramolecular nanostructures with shape diversity ranging from spheres to cylinders, twisted ribbons, belts, and tubes. Understanding the self-assembly mechanisms to control dimensions and shapes of the nanostructures remains a grand challenge."

The news reporters obtained a quote from the research from Northwestern University, "We report here on a systematic study of peptide amphiphiles containing valine-glutamic acid dimeric repeats known to promote self-assembly into belt-like flat assemblies. We find that the lateral growth of the assemblies can be controlled in the range of 100 nm down to 10 nm as the number of dimeric repeats is increased from two to six. Using circular dichroism, the degree of ?-sheet twisting within the supramolecular assemblies was found to be directly proportional to the number of dimeric repeats in the PA molecule. Interestingly, as twisting increased, a threshold is reached where cylinders rather than flat assemblies become the dominant morphology. We also show that in the belt regime, the width of the nanostructures can be decreased by raising the pH to increase charge density and therefore electrostatic repulsion among glutamic acid residues."

According to the news reporters, the research concluded: "The control of size and shape of these nanostructures should affect their functions in biological signaling and drug delivery."

For more information on this research see: Tuning nanostructure dimensions with supramolecular twisting. The Journal of Physical Chemistry B, 2013;117(16):4604-10 (see also Proteomics).

Our news correspondents report that additional information may be obtained by contacting T.J. Moyer, Dept. of Materials Science, Northwestern University, Evanston, Illinois 60208, United States. Additional authors for this research include H. Cui and S.I Stupp.

Keywords for this news article include: Evanston, Illinois, Peptides, Proteins, Proteomics, United States, Nanotechnology, Supramolecular, 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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