Unlocking the Potential of Plasma Proteomics

Unlocking the Potential of Plasma Proteomics Unlocking the Potential of Plasma Proteomics If you would like our editorial team to create a title for you based on your content, please tick this box and our in-house team of experienced science writers will create this for you ☐ Plasma proteomic technologies are evolving quickly and are crucial for biomedical research. This study presents a technical evaluation of six prominent plasma proteomic technologies. These methods were assessed based on factors such as proteomic depth, reproducibility, linearity, resistance to lipid interference, and limits of detection and quantification. A total of 618 LC-MS/MS experiments and 93 assays were performed. The method with the greatest proteomic depth identified around 4,500 proteins, while another method detected about 2,600 proteins. Other methods detected between 500 and 2,200 proteins. Some methods demonstrated strong reproducibility, while others exhibited more variability. All mass spectrometry-based techniques showed good linearity with spiked-in C-Reactive Protein (CRP), though CRP was not detected by one assay. None of the methods were affected by lipid interference. The top method for detecting and quantifying proteins had more than double the number of quantifiable proteins at both the limit of detection and limit of quantification compared to other methods. Another method showed similar performance to the others for the limit of detection but performed worse for the limit of quantification. Finally, the ability of these technologies to detect differences between healthy and cancer groups in a non-small cell lung cancer cohort was assessed. Plasma proteomic technologies are evolving quickly and are crucial for biomedical research. This webinar will compare six leading plasma proteomic technologies, providing insights into their performance and applications. Our expert speaker will outline how mass spectrometry-based methods and affinity-based approaches were evaluated for proteomic depth, reproducibility and their ability to detect disease-related biomarkers. They will also highlight how these methods contribute to advancing the understanding of disease biology and improving diagnostic strategies, including in cancer research. Josh Coon, PhD Professor of Biomolecular Chemistry and Chemistry He/Him Other: University of Wisconsin jcoon@chem.wisc.edu Dr. Coon is a professor of Chemistry and Biomolecular Chemistry at the University of Wisconsin-Madison, where he also holds the Thomas and Margaret Pyle Chair at the Morgridge Institute for Research. He earned his B.S. from Central Michigan University in 1998 and his Ph.D. from the University of Florida in 2002, followed by a postdoctoral fellowship at the University of Virginia from 2003 to 2005. Dr. Coon’s research focuses on bioanalytical chemistry, mass spectrometry, and proteomics. He co-developed electron-transfer dissociation (ETD), a technique that has advanced proteomic analysis. His work aims to improve mass spectrometric technologies to enable comprehensive analysis of proteins and metabolites, advancing biomedical research. Dr. Coon has received numerous accolades, including the Biemann Medal in 2012, the Pittsburgh Conference Achievement Award in 2010, and the Ken Standing Award in 2009. He was named one of "Tomorrow’s PI’s" by Genome Technology magazine in 2006. Dr. Coon also directs the NIGMS National Center for Quantitative Biology of Complex Systems.