By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Proteins have been published. According to news reporting from Seoul, South Korea, by NewsRx journalists, research stated, "Self-assembly of amyloid nanofiber is associated with both functional biological and pathological processes such as those in neurodegenerative diseases. Despite intensive studies, the stochastic nature of the process has made it difficult to elucidate a molecular mechanism for the key amyloid nucleation event."
The news correspondents obtained a quote from the research from the School of Computational Science, "Here we investigated nucleation of the silk-elastin-like peptide (SELP) amyloid using time-lapse lateral force microscopy (LFM). By repeated scanning of a single line on a SELP-coated mica surface, we observed a sudden stepwise height increase. This corresponds to nucleation of an amyloid fiber, which subsequently grew perpendicular to the scanning direction. The lateral force profiles followed either a worm-like chain model or an exponential function, suggesting that the atomic force microscopy (AFM) tip stretches a single or multiple SELP molecules along the scanning direction. The probability of nucleation correlated with the maximum stretching force and extension, implying that stretching of SELP molecules is a key molecular event for amyloid nucleation."
According to the news reporters, the research concluded: "The mechanically induced nucleation allows for positional and directional control of amyloid assembly in vitro, which we demonstrate by generating single nanofibers at predetermined nucleation sites."
For more information on this research see: Direct Observation of Amyloid Nucleation under Nanomechanical Stretching. ACS Nano, 2013;7(9):7734-7743. 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 journalists report that additional information may be obtained by contacting N. Varongchayakul, Korea Inst Adv Study, Sch Computat Sci, Seoul 130722, South Korea. Additional authors for this research include S. Johnson, T. Quabili, J. Cappello, H. Ghandehari, S.D. Solares, W. Hwang and J. Seog (see also Proteins).
Keywords for this news article include: Asia, Seoul, Amyloid, Proteins, South Korea
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