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Studies from State Key Laboratory of Surface Physics Have Provided New Information about Peptides and Proteins

May 13, 2014



By a News Reporter-Staff News Editor at Life Science Weekly -- Research findings on Peptides and Proteins are discussed in a new report. According to news reporting originating from Shanghai, People's Republic of China, by NewsRx correspondents, research stated, "Understanding the nature of the self-assembly of peptide nanostructures at the molecular level is critical for rational design of functional bio-nanomaterials. Recent experimental studies have shown that triphenylalanine(FFF)-based peptides can self-assemble into solid plate-like nanostructures and nanospheres, which are different from the hollow nanovesicles and nanotubes formed by diphenylalanine(FF)-based peptides."

Our news editors obtained a quote from the research from the State Key Laboratory of Surface Physics, "In spite of extensive studies, the assembly mechanism and the molecular basis for the structural differences between FFF and FF nanostructures remain poorly understood. In this work, we first investigate the assembly process and the structural features of FFF nanostructures using coarse-grained molecular dynamics simulations, and then compare them with FF nanostructures. We find that FFF peptides spontaneously assemble into solid nanometer-sized nanospheres and nanorods with substantial ?-sheet contents, consistent with the structural properties of hundred-nanometer-sized FFF nano-plates characterized by FT-IR spectroscopy. Distinct from the formation mechanism of water-filled FF nanovesicles and nanotubes reported in our previous study, intermediate bilayers are not observed during the self-assembly process of FFF nanospheres and nanorods. The peptides in FFF nanostructures are predominantly anti-parallel-aligned, which can form larger sizes of ?-sheet-like structures than the FF counterparts. In contrast, FF peptides exhibit lipid-like assembly behavior and assemble into bilayered nanostructures. Furthermore, although the self-assembly of FF and FFF peptides is mostly driven by side chain-side chain (SC-SC) aromatic stacking interactions, the main chain-main chain (MC-MC) interactions also play an important role in the formation of fine structures of the assemblies. The delicate interplay between MC-MC and SC-SC interactions results in the different nanostructures formed by the two peptides."

According to the news editors, the research concluded: "These findings provide new insights into the structure and self-assembly pathway of di-/tri-phenylalanine peptide assemblies, which might be helpful for the design of bioinspired nanostructures."

For more information on this research see: Triphenylalanine peptides self-assemble into nanospheres and nanorods that are different from the nanovesicles and nanotubes formed by diphenylalanine peptides. Nanoscale, 2014;6(5):2800-11. (Royal Society of Chemistry - www.rsc.org/; Nanoscale - pubs.rsc.org/en/journals/journalissues/nr)

The news editors report that additional information may be obtained by contacting C. Guo, State Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences (MOE), 220 Handan Road, Shanghai, 200433, People's Republic of China. Additional authors for this research include Y. Luo, R. Zhou and G. Wei (see also Peptides and Proteins).

Keywords for this news article include: Asia, Nanorod, Shanghai, Nanotube, Amino Acids, Nanostructural, Nanostructures, Nanotechnology, Emerging Technologies, Peptides and Proteins, People's Republic of China.

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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