title: Is isolation of comprehensive human plasma peptidomes an achievable quest?
abstract: The low molecular weight (LMW; <10kDa)* plasma peptidome has been considered a source of useful diagnostic biomarkers and potentially therapeutic molecules, as it contains many cytokines, peptide hormones, endogenous peptide products and potentially bioactive fragments derived from the parent proteome. The small size of the peptides allows them almost unrestricted vascular and interstitial access, and hence distribution across blood-brain barriers, tumour and other vascular permeability barriers. Therefore, the peptidome may carry specific signatures or fingerprints of an individual's health, wellbeing or disease status. This occurs primarily because of the advantage the peptidome has in being readily accessible in human blood and/or other biofluids. However, the co-expression of highly abundant proteins (>10kDa) and other factors present inherently in human plasma make direct analysis of the blood peptidome one of the most challenging tasks faced in contemporary analytical biochemistry. A comprehensive compendium of extraction and fractionation tools has been collected concerning the isolation and micromanipulation of peptides. However, the search for a reliable, accurate and reproducible single or combinatorial separation process for capturing and analysing the plasma peptidome remains a challenge. This review outlines current techniques used for the separation and detection of plasma peptides and suggests potential avenues for future investigation. This article is part of a Special Issue entitled: HUPO 2014.
authors.affiliation: Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, NSW 2109, Australia.
authors.forename: S
authors.initials: S
authors.lastname: Mahboob
authors.affiliation: Department of Chemistry and Biomolecular Sciences, Faculty of Science, Macquarie University, NSW 2109, Australia.
authors.forename: A
authors.initials: A
authors.lastname: Mohamedali
authors.affiliation: Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, NSW 2109, Australia.
authors.forename: S B
authors.initials: SB
authors.lastname: Ahn
authors.affiliation: Protagen AG, 44227 Dortmund Germany.
authors.forename: P
authors.initials: P
authors.lastname: Schulz-Knappe
authors.affiliation: Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
authors.forename: E
authors.initials: E
authors.lastname: Nice
authors.affiliation: Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, NSW 2109, Australia. Electronic address: mark.baker@mq.edu.au.
authors.forename: M S
authors.initials: MS
authors.lastname: Baker
mesh_terms: D001798:Blood Proteins / Q000378:metabolism*; D006801:Humans; D010455:Peptides / Q000097:blood*; D020543:Proteome / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*
chemical_list: D001798:Blood Proteins; D010455:Peptides; D020543:Proteome
keywords: Human plasma; Peptidome; Peptidomics; Separation