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Advancing Collision-Induced Affinity Selection Mass Spectrometry for Quantitative Ligand Analysis in Complex Mixtures.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: Advancing Collision-Induced Affinity Selection Mass Spectrometry for Quantitative Ligand Analysis in Complex Mixtures.
Συγγραφείς: Xue X; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia., Quinn RJ; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia., Rehm BHA; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia.; Centre for Cell Factories and Biopolymers, Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia., Day CJ; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia., Jennings MP; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia., McBroom J; School of Environment and Science, Griffith University, Nathan, 4111 Brisbane, Queensland, Australia., Littler DR; Infection and Immunity Program & Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton 3800, Victoria, Australia., Liu M; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia.; School of Environment and Science, Griffith University, Nathan, 4111 Brisbane, Queensland, Australia.
Πηγή: Analytical chemistry [Anal Chem] 2026 Mar 17; Vol. 98 (10), pp. 7247-7261. Date of Electronic Publication: 2026 Mar 03.
Τύπος έκδοσης: Journal Article; Research Support, Non-U.S. Gov't
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370536 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-6882 (Electronic) Linking ISSN: 00032700 NLM ISO Abbreviation: Anal Chem Subsets: MEDLINE
Imprint Name(s): Original Publication: Washington, American Chemical Society.
Ιατρικοί όροι (MeSH): Complex Mixtures*/chemistry , Complex Mixtures*/analysis , Mass Spectrometry*/methods , Proteins*/chemistry , Proteins*/metabolism, Spectrometry, Mass, Electrospray Ionization/methods ; Ligands
Περίληψη: Native mass spectrometry (MS) is a powerful technique for studying protein-ligand interactions in their native states by employing soft electrospray ionization (ESI). It enables the direct observation of all species in equilibrium within a solution. Building on these advantages, Collision-Induced Affinity Selection MS (CIAS-MS) was introduced as an alternative approach, incorporating quadrupole mass selection, controlled complex dissociation, and ligand detection to enhance the study of protein-ligand interactions. This method retains the native ionization properties of proteins while enabling high-sensitivity detection of released ligands. This study presents an optimized CIAS-MS platform for improved ligand binding detection and quantitative affinity ranking. The integration of both positive and negative ion modes significantly broadens the detection of structurally diverse ligands, overcoming biases from single-mode analysis. More importantly, the collision-induced dissociation (CID) slope, derived from dissociation curves, is introduced as a robust parameter for affinity ranking. Unlike absolute intensities or dissociation thresholds, the CID slope reflects solution-phase affinity order across ligands and remains accurate in highly complex backgrounds, including 100-compound mixtures and bacterial lysates. These advances highlight the robustness of CIAS-MS for detecting bound ligands and ranking their affinities even under challenging conditions where traditional native MS fails. These findings establish CIAS-MS as a scalable and efficient platform for high-throughput ligand discovery and proteome-wide target engagement studies, offering a powerful addition to the biophysical toolkit for modern drug discovery.
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Int J Mass Spectrom. 2020 Dec;458:. (PMID: 33162786)
Curr Opin Chem Biol. 2022 Aug;69:102157. (PMID: 35580377)
J Am Soc Mass Spectrom. 2007 Sep;18(9):1605-11. (PMID: 17629493)
Sci Rep. 2016 May 10;6:25769. (PMID: 27161290)
Fundam Clin Pharmacol. 2008 Dec;22(6):633-48. (PMID: 19049668)
Protein Sci. 2016 Nov;25(11):1924-1941. (PMID: 27522064)
Chem Rev. 2008 Mar;108(3):946-1051. (PMID: 18335973)
Prog Nucl Magn Reson Spectrosc. 2023 Nov-Dec;138-139:52-69. (PMID: 38065668)
Molecules. 2020 May 21;25(10):. (PMID: 32455540)
Curr Opin Biotechnol. 1997 Feb 1;8(1):31-5. (PMID: 9013658)
J Biomol Screen. 2006 Oct;11(7):782-91. (PMID: 16858005)
Curr Opin Biotechnol. 1997 Aug;8(4):498-502. (PMID: 9265731)
J Am Chem Soc. 2021 Dec 22;143(50):21379-21387. (PMID: 34886668)
Methods Enzymol. 2005;402:148-85. (PMID: 16401509)
J Biomol Screen. 2008 Apr;13(4):265-75. (PMID: 18349420)
Anal Chem. 2024 Dec 3;96(48):18932-18938. (PMID: 39556209)
Molecules. 2024 Oct 29;29(21):. (PMID: 39519740)
Expert Opin Drug Discov. 2015;10(9):975-89. (PMID: 26177814)
J Nat Prod. 2023 Dec 22;86(12):2630-2637. (PMID: 37993134)
Ther Drug Monit. 1993 Dec;15(6):563-9. (PMID: 8122295)
ACS Omega. 2022 Apr 14;7(16):13925-13931. (PMID: 35559183)
ACS Pharmacol Transl Sci. 2023 Mar 07;6(4):578-586. (PMID: 37082753)
ACS Chem Biol. 2024 Mar 15;19(3):763-773. (PMID: 38449446)
ACS Cent Sci. 2019 Feb 27;5(2):308-318. (PMID: 30834319)
J Am Soc Mass Spectrom. 2016 Jun;27(6):1099-104. (PMID: 27106602)
Nat Protoc. 2020 Feb;15(2):236-265. (PMID: 31942081)
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Anal Chem. 2004 Aug 1;76(15):4325-31. (PMID: 15283568)
ACS Infect Dis. 2018 Apr 13;4(4):431-444. (PMID: 29436819)
J Am Soc Mass Spectrom. 2025 Feb 05;36(2):355-367. (PMID: 39812073)
ACS Omega. 2024 Oct 31;9(45):45309-45318. (PMID: 39554431)
Methods Appl Fluoresc. 2022 Jul 28;10(4):. (PMID: 35856854)
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Elife. 2020 Aug 06;9:. (PMID: 32758356)
Mol Biol Cell. 2013 Apr;24(7):883-6. (PMID: 23533209)
Substance Nomenclature: 0 (Ligands)
0 (Complex Mixtures)
0 (Proteins)
Entry Date(s): Date Created: 20260303 Date Completed: 20260710 Latest Revision: 20260813
Update Code: 20260813
PubMed Central ID: PMC13000879
DOI: 10.1021/acs.analchem.5c06115
PMID: 41775340
Βάση Δεδομένων: MEDLINE
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  Data: Advancing Collision-Induced Affinity Selection Mass Spectrometry for Quantitative Ligand Analysis in Complex Mixtures.
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  Data: <searchLink fieldCode="AU" term="%22Xue+X%22">Xue X</searchLink>; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia.<br /><searchLink fieldCode="AU" term="%22Quinn+RJ%22">Quinn RJ</searchLink>; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia.<br /><searchLink fieldCode="AU" term="%22Rehm+BHA%22">Rehm BHA</searchLink>; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia.; Centre for Cell Factories and Biopolymers, Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia.<br /><searchLink fieldCode="AU" term="%22Day+CJ%22">Day CJ</searchLink>; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia.<br /><searchLink fieldCode="AU" term="%22Jennings+MP%22">Jennings MP</searchLink>; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia.<br /><searchLink fieldCode="AU" term="%22McBroom+J%22">McBroom J</searchLink>; School of Environment and Science, Griffith University, Nathan, 4111 Brisbane, Queensland, Australia.<br /><searchLink fieldCode="AU" term="%22Littler+DR%22">Littler DR</searchLink>; Infection and Immunity Program & Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton 3800, Victoria, Australia.<br /><searchLink fieldCode="AU" term="%22Liu+M%22">Liu M</searchLink>; Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia.; School of Environment and Science, Griffith University, Nathan, 4111 Brisbane, Queensland, Australia.
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  Data: <searchLink fieldCode="MM" term="%22Complex+Mixtures%22">Complex Mixtures*</searchLink>/<searchLink fieldCode="MM" term="%22Complex+Mixtures+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Complex+Mixtures%22">Complex Mixtures*</searchLink>/<searchLink fieldCode="MM" term="%22Complex+Mixtures+analysis%22">analysis</searchLink> <br /><searchLink fieldCode="MM" term="%22Mass+Spectrometry%22">Mass Spectrometry*</searchLink>/<searchLink fieldCode="MM" term="%22Mass+Spectrometry+methods%22">methods</searchLink> <br /><searchLink fieldCode="MM" term="%22Proteins%22">Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Proteins+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Proteins%22">Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Proteins+metabolism%22">metabolism</searchLink><br /><searchLink fieldCode="MH" term="%22Spectrometry%2C+Mass%2C+Electrospray+Ionization%22">Spectrometry, Mass, Electrospray Ionization</searchLink>/<searchLink fieldCode="MH" term="%22Spectrometry%2C+Mass%2C+Electrospray+Ionization+methods%22">methods</searchLink> ; <searchLink fieldCode="MH" term="%22Ligands%22">Ligands</searchLink>
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  Data: Native mass spectrometry (MS) is a powerful technique for studying protein-ligand interactions in their native states by employing soft electrospray ionization (ESI). It enables the direct observation of all species in equilibrium within a solution. Building on these advantages, Collision-Induced Affinity Selection MS (CIAS-MS) was introduced as an alternative approach, incorporating quadrupole mass selection, controlled complex dissociation, and ligand detection to enhance the study of protein-ligand interactions. This method retains the native ionization properties of proteins while enabling high-sensitivity detection of released ligands. This study presents an optimized CIAS-MS platform for improved ligand binding detection and quantitative affinity ranking. The integration of both positive and negative ion modes significantly broadens the detection of structurally diverse ligands, overcoming biases from single-mode analysis. More importantly, the collision-induced dissociation (CID) slope, derived from dissociation curves, is introduced as a robust parameter for affinity ranking. Unlike absolute intensities or dissociation thresholds, the CID slope reflects solution-phase affinity order across ligands and remains accurate in highly complex backgrounds, including 100-compound mixtures and bacterial lysates. These advances highlight the robustness of CIAS-MS for detecting bound ligands and ranking their affinities even under challenging conditions where traditional native MS fails. These findings establish CIAS-MS as a scalable and efficient platform for high-throughput ligand discovery and proteome-wide target engagement studies, offering a powerful addition to the biophysical toolkit for modern drug discovery.
– Name: Ref
  Label: References
  Group: RefInfo
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              Value: 1520-6882
          Numbering:
            – Type: volume
              Value: 98
            – Type: issue
              Value: 10
          Titles:
            – TitleFull: Analytical chemistry
              Type: main
ResultId 1