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New Peptides and Proteins Study Results Reported from Bhabha Atomic Research Centre (Small-angle neutron scattering study of differences in phase...

July 8, 2014



New Peptides and Proteins Study Results Reported from Bhabha Atomic Research Centre (Small-angle neutron scattering study of differences in phase behavior of silica nanoparticles in the presence of lysozyme and bovine serum albumin proteins)

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 from Mumbai, India, by NewsRx journalists, research stated, "The differences in phase behavior of anionic silica nanoparticles (88 A) in the presence of two globular proteins [cationic lysozyme (molecular weight (MW) 14.7 kD) and anionic bovine serum albumin (BSA) (MW 66.4 kD)] have been studied by small-angle neutron scattering. The measurements were carried out on a fixed concentration (1 wt %) of Ludox silica nanoparticles with varying concentrations of proteins (0-5 wt %) at pH = 7."

The news correspondents obtained a quote from the research from Bhabha Atomic Research Centre, "It is found that, despite having different natures (opposite charges), both proteins can render to the same kind of aggregation of silica nanoparticles. However, the concentration regions over which the aggregation is observed are widely different for the two proteins. Lysozyme with very small amounts (e.g., 0.01 wt %) leads to the aggregation of silica nanoparticles. On the other hand, silica nanoparticles coexist with BSA as independent entities at low protein concentrations and turn to aggregates at high protein concentrations (>1 wt %). In the case of lysozyme, the charge neutralization by the protein on the nanoparticles gives rise to the protein-mediated aggregation of the nanoparticles. The nanoparticle aggregates coexist with unaggregated nanoparticles at low protein concentrations, whereas, they coexist with a free protein at higher protein concentrations. For BSA, the nonadsorbing nature of the protein produces the depletion force that causes the aggregation of the nanoparticles at higher protein concentrations. The evolution of the interaction is modeled by the two Yukawa potential, taking account of both attractive and repulsive terms of the interaction in these systems. The nanoparticle aggregation is found to be governed by the short-range attraction for lysozyme and the long-range attraction for BSA."

According to the news reporters, the research concluded: "The aggregates are characterized by the diffusion limited aggregate type of mass fractal morphology."

For more information on this research see: Small-angle neutron scattering study of differences in phase behavior of silica nanoparticles in the presence of lysozyme and bovine serum albumin proteins. Physical Review E, Statistical, Nonlinear, and Soft Matter Physics, 2014;89(3):032304 (see also Peptides and Proteins).

Our news journalists report that additional information may be obtained by contacting I. Yadav, Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai 400 085, India. Additional authors for this research include S. Kumar, V.K. Aswal and J. Kohlbrecher.

Keywords for this news article include: Asia, India, Mumbai, Lysozyme, Amino Acids, Nanoparticle, Blood Proteins, Nanotechnology, Acute Phase Proteins, Bovine Serum Albumin, Emerging Technologies, Peptides and Proteins.

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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