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Biology subjects

Fisher, T. D.

Publications and source records attributed to Fisher, T. D..

2 recordsLinked to original sources

Targeted Analysis of >1500 Plasma Proteoforms via Individual Ion Mass Spectrometry

Plasma proteomics has long sought to accessibly sense human biology, precisely detect disease states, and advance diagnostics through clinical translation. In recent years, companies with defined panels such as Olink and Somascan have entered the field to complement bottom-up mass spectrometry (BUP). This study leverages a novel mass spectrometry platform to capture targeted proteoform information lost by mainline antibody-, aptamer-, and BUP-driven workflows. The Plasma Proteoform Assay (PPA) uses Individual Ion Mass Spectrometry (I{superscript 2}MS) to resolve mixtures of intact proteins presented by direct injection. Two proteoform panels, PPA 526 and PPA 1514, were defined from human plasma samples obtained from 81 individuals. The panels quantify 526 proteoforms derived from 59 genes and 1,514 proteoforms from 155 genes, respectively. Reproducibility for both panels showed coefficients of variation below 20% for most proteoforms (59-80%). PPA was benchmarked in studies including subjects with hepatic cirrhosis (N=30) and resilient agers carrying a SERPINE1 (PAI 1) mutation (N=27). PPA signatures distinguished SERPINE1 mutation carriers from affected individuals and provided sufficient resolution to discriminate among cirrhosis disease stages. In summary, we present PPA 526 and PPA 1514, the first scalable plasma proteoform panels capable of tracking hundreds to thousands of targets in a few minutes per sample.

biochemistry↗

Next-Generation Protein Sequencing and individual ion mass spectrometry enable complementary analysis of interleukin-6

The vast complexity of the proteome currently overwhelms any single analytical technology in capturing the full spectrum of proteoform diversity. In this study, we evaluated the complementarity of two cutting-edge proteomic technologies--single-molecule protein sequencing and individual ion mass spectrometry--for analyzing recombinant human IL-6 (rhIL-6) at the amino acid, peptide, and intact proteoform levels. For single-molecule protein sequencing, we employ the recently released Platinum(R) instrument. Next-Generation Protein Sequencing (NGPS) on Platinum utilizes cycles of N-terminal amino acid recognizer binding and aminopeptidase cleavage to enable parallelized sequencing of single peptide molecules. We found that NGPS produces single amino acid coverage of multiple key regions of IL-6, including two peptides within helices A and C which harbor residues that reportedly impact IL-6 function. For top-down proteoform evaluation, we use individual ion mass spectrometry (I2MS), a highly parallelized orbitrap-based charge detection MS platform. Single ion detection of gas-phase fragmentation products (I2MS2) gives significant sequence coverage in key regions in IL-6, including two regions within helices B and D that are involved in IL-6 signaling. Together, these complementary technologies deliver a combined 52% sequence coverage, offering a more complete view of IL-6 structural and functional diversity than either technology alone. This study highlights the synergy of complementary protein detection methods to more comprehensively cover protein segments relevant to biological interactions. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=114 SRC="FIGDIR/small/637157v1_ufig1.gif" ALT="Figure 1"> View larger version (39K): org.highwire.dtl.DTLVardef@82d72aorg.highwire.dtl.DTLVardef@1fc39f3org.highwire.dtl.DTLVardef@40a677org.highwire.dtl.DTLVardef@70f6c3_HPS_FORMAT_FIGEXP M_FIG C_FIG

biochemistry↗