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ORIGINAL RESEARCH article

Front. Cell Dev. Biol.
Sec. Cellular Biochemistry
Volume 12 - 2024 | doi: 10.3389/fcell.2024.1504098
This article is part of the Research Topic Advancements in Proteomics and PTMomics: Unveiling Mechanistic Insights and Targeted Therapies for Metabolic Diseases View all 3 articles

Protein 'Purity', Proteoforms, and the Albuminome: Critical Observations on Proteome and Systems Complexity

Provisionally accepted
Breyer-Lynne Woodland Breyer-Lynne Woodland 1Jens R. Coorssen Jens R. Coorssen 2*Matthew P Padula Matthew P Padula 1*
  • 1 University of Technology Sydney, Sydney, Australia
  • 2 Brock University, St. Catharines, Ontario, Canada

The final, formatted version of the article will be published soon.

    The identification of effective, selective biomarkers and therapeutics is dependent on truly deep, comprehensive analysis of proteomes at the proteoform level. Using bovine serum albumin (BSA) isolated by two different protocols, cold ethanol fractionation (CEF) and heat shock fractionation (HSF), the data highlight several concerns regarding proteome analyses using currently popular analytical approaches and what it means to purify a 'protein' if the isolate consists of a wide variety of proteoforms and/or co-purifying species. Failure to widely recognize and accept proteome complexity has likely delayed the identification of effective biomarkers and new, more selective drug targets. Integrative top-down proteomics (iTDP) is the most logical available analytical technique to effectively provide the necessary critical depth and breadth for complex proteome analyses. Routine analyses at the level of proteoforms will provide the much-needed data for the development and validation of selective biomarkers and drugs, including biologics.

    Keywords: biologics1, biomarkers2, bovine serum albumin3, integrative top-down proteomics4, proteoforms5, tandem mass spectrometry6, therapeutics7, two-dimensional gel electrophoresis8

    Received: 01 Oct 2024; Accepted: 13 Nov 2024.

    Copyright: © 2024 Woodland, Coorssen and Padula. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence:
    Jens R. Coorssen, Brock University, St. Catharines, L2S 3A1, Ontario, Canada
    Matthew P Padula, University of Technology Sydney, Sydney, Australia

    Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.