developed a novel technology: Nanotrap® particles, which are designed to capture, concentrate, and protect demonstrating that Nanotrap® particles are able to capture live infectious virus, viral RNA, and viral proteins Capture is possible even in complex mixtures such as serum and allows the concentration and protection

PLoS ONE 2014 The Use of Nanotrap® Particles Technology in Capturing HIV-1 Virions and Viral Proteins This study demonstrates that majority of HIV-1 virions in culture supernatants and Tat/Nef proteins spiked Intracellular Nef protein was captured by NT080, while membrane-associated Nef was captured by NT086 and we propose to use this technology as a platform to enhance HIV-1 detection by concentrating viral proteins

Replication ​ The implementation of new antiretroviral therapies targeting transcription of early viral proteins Finally, we observed that neuronal cultures treated with Tat protein are protected from Tat-mediated

Furthermore, detection may be hindered by high abundant proteins such as albumin. drastically improve the detection of the RVFV nucleoprotein (NP), the most abundant and widely used viral protein

identification using shotgun proteomics approach Serum low-molecular weight (LMW) proteins potentially In this study three different methods, i.e. hydrogel nanoparticles, Proteominer(®) peptide ligand affinity A shotgun proteomics approach was adopted, with in-solution proteolytic digestion of the whole protein Data analysis, focusing on the LMW proteome (MW ≤ 40 kDa), has shown that the hydrogel nanoparticles for Proteominer(®) beads and Sartorius Vivaspin(®) device, respectively.

Journal of Proteome Research, May 29, 2012 Over the past few years, mass spectrometry has emerged as Application of mass spectrometry to protein and peptide measurement can provide advantages including Furthermore, an important caveat of SRM-based assays for proteins is that many low-abundance analytes reproducible with coefficients of variation of less than 30% for the measurement of important clinical proteins

spectrometry because they exist in body fluids in very low concentrations, are masked by high-abundance proteins buoyant, core–shell hydrogel nanoparticles containing novel high affinity reactive chemical baits for protein novel) molecular baits showed preferential high affinities (KD < 10–11 M) for specific low-abundance protein Proteins and peptides entered the core to be captured with high affinity by baits immobilized in the Nanoparticles effectively protected interleukin-6 from enzymatic degradation in sweat and increased the

were evaluated as a biomaterial to amplify the sensitivity of urine testing for infectious disease proteins The dyes act as affinity baits towards protein analytes in solution.

Purpose: We sought to determine whether low‐abundant serum proteins related to apoptotic pathways could Hydrogel core shell nanoparticles, a new technology capable of selectively entrapping low molecular weight proteins and protecting them from enzymatic degradation, were used to capture candidate serum biomarkers. Results: Among a panel of analyzed serum proteins, Bak was differentially expressed between nevi and Conclusions: Our study links serum proteome analysis with confocal microscopic clinical in vivo histologic

Detection Markers Using a Novel Nanoparticle Biomarker Capture Technology Current efforts to identify protein barrier of the vasculature, which provides opportunity to measure disease microenvironment-associated protein However, identifying useful protein biomarkers (peptidomic or not) which could be useful to detect early technology that can, in one step, capture, concentrate, and separate the peptidome from high-abundance blood proteins

nanoparticles can perform, in one step, (1) complete harvesting of all solution phase target analytes, (2) full protection

Hydrogel Particles Harvest, Concentrate and Preserve Labile Low Abundance Biomarkers Background: The blood proteome a) candidate biomarkers exist at extremely low concentrations in blood; b) high abundance resident proteins PDGF, spiked in human serum, was completely sequestered from its carrier protein albumin, concentrated Particle sequestered PDGF was fully protected from exogenously added tryptic degradation. Beyond PDGF, the sequestration and protection from degradation for a series of additional very low abundance