By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Proteins have been published. According to news reporting originating in Zurich, Switzerland, by NewsRx journalists, research stated, "We report on the synthesis and magnetic-responsive behavior of hybrids formed by dispersing negatively charged iron oxide (Fe3O4) magnetic nanoparticles in positively charged ?-lactoglobulin protein solutions at acidic pH, followed by heating at high temperatures. Depending on the pH used, different hybrid aggregates can be obtained, such as nanoparticle-modified amyloid fibrils (pH 3) and spherical nanoclusters (pH 4.5)."
The news reporters obtained a quote from the research from the Department of Health Science and Technology, "We investigate the effect of magnetic fields of varying strengths (0-5 T) on the alignment of these Fe3O4-modified amyloid fibrils and spherical nanoclusters using a combination of scattering, birefringence and microscopic techniques and we find a strong alignment of the hybrids upon increasing the intensity of the magnetic field, which we quantify via 2D and 3D order parameters. We also demonstrate the possibility of controlling magnetically the sol-gel behavior of these hybrids: addition of salt (NaCl, 150 mM) to a solution containing nanoparticles modified with ?-lactoglobulin amyloid fibrils (2 wt % fibrils modified with 0.6 wt % Fe3O4 nanoparticles) induces first the formation of a reversible gel, which can then be converted back to solution upon application of a moderate magnetic field of 1.1 T."
According to the news reporters, the research concluded: "These hybrids offer a new appealing functional colloidal system in which the aggregation, orientational order and rheological behavior can be efficiently controlled in a purely noninvasive way by external magnetic fields of weak intensity."
For more information on this research see: Magnetic-responsive hybrids of Fe3O4 nanoparticles with ?-lactoglobulin amyloid fibrils and nanoclusters. Acs Nano, 2013;7(7):6146-55. (American Chemical Society - www.acs.org; Acs Nano - www.pubs.acs.org/journal/ancac3)
Our news correspondents report that additional information may be obtained by contacting S. Bolisetty, Dept. of Health Science and Technology, Food and Soft Materials Laboratory, ETH Zurich, Schmelzbergstrasse 9, LFO-E22, CH-8092 Zurich, Switzerland. Additional authors for this research include J.J. Vallooran, J. Adamcik and R. Mezzenga (see also Proteins).
Keywords for this news article include: Zurich, Europe, Amyloid, Switzerland, Nanoparticle, Milk Proteins, Lactoglobulins, Nanotechnology, Emerging Technologies.
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