By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Peptides and Proteins have been published. According to news reporting originating in Aurora, Colorado, by NewsRx journalists, research stated, "The potential applications of nanomaterials as drug delivery systems and in other products continue to expand. Upon introduction into physiological environments and driven by energetics, nanomaterials readily associate proteins forming a protein corona (PC) on their surface."
The news reporters obtained a quote from the research from the University of Colorado, "This PC influences the nanomaterial's surface characteristics and may impact their interaction with cells. To determine the biological impact of nanomaterial exposure as well as nanotherapeutic applications, it is necessary to understand PC formation. Utilizing a label-free mass spectrometry-based proteomics approach, we examined the composition of the PC for a set of four silver nanoparticles (AgNPs) including citrate-stabilized and polyvinlypyrrolidone-stabilized (PVP) colloidal silver (20 or 110 nm diameter). To simulate cell culture conditions, AgNPs were incubated for 1 h in Dulbecco's Modified Eagle Medium supplemented with 10% fetal bovine serum, washed, coronal proteins solubilized, and proteins identified and quantified by label-free LC-MS/MS. To determine which attributes influence PC formation, the AgNPs were characterized in both water and cell culture media with 10% FBS. All AgNPs associated a common subset of 11 proteins including albumin, apolipoproteins, keratins, and other serum proteins. 110 nm citrate-and PVP-stabilized AgNPs were found to bind the greatest number of proteins (79 and 85 respectively) compared to 20 nm citrate-and PVP-stabilized AgNPs (45 and 48 respectively), suggesting a difference in PC formation based on surface curvature. While no relationships were found for other protein parameters (isoelectric point or aliphatic index), the PC on 20 nm AgNPs (PVP and citrate) consisted of more hydrophobic proteins compared to 110 nm AgNPs implying that this class of proteins are more receptive to curvature-induced folding and crowding in exchange for an increased hydration in the aqueous environment."
According to the news reporters, the research concluded: "These observations demonstrate the significance of electrostatic and hydrophobic interactions in the formation of the PC which may have broad biological and toxicological implications."
For more information on this research see: Silver nanoparticle protein corona composition in cell culture media. Plos One, 2013;8(9):e74001. (Public Library of Science - www.plos.org; Plos One - www.plosone.org)
Our news correspondents report that additional information may be obtained by contacting J.H. Shannahan, Dept. of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, Colorado, United States. Additional authors for this research include X. Lai, P.C. Ke, R. Podila, J.M. Brown and F.A Witzmann (see also Peptides and Proteins).
Keywords for this news article include: Aurora, Colorado, Amino Acids, Nanomaterial, United States, Nanotechnology, Emerging Technologies, Peptides and Proteins, North and Central America.
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