Cited by 96Mass Spectrometry Techniques and ApplicationsChemical Synthesis and AnalysisAdvanced Proteomics Techniques and Applications

Affinity Selection and Mass Spectrometry-Based Strategies to Identify Lead Compounds in Combinatorial Libraries

Kaur, Surinder, McGuire, Lisa, Tang, Dazhi, Dollinger, Gavin, Huebner, Verena·1997·Journal of Protein Chemistry

Abstract

The screening of diverse libraries of small molecules created by combinatorial synthetic methods is a recent development which has the potential to accelerate the identification of lead compounds in drug discovery. We have developed a direct and rapid method to identify lead compounds in libraries involving affinity selection and mass spectrometry. In our strategy, the receptor or target molecule of interest is used to isolate the active components from the library physically, followed by direct structural identification of the active compounds bound to the target molecule by mass spectrometry. In a drug design strategy, structurally diverse libraries can be used for the initial identification of lead compounds. Once lead compounds have been identified, libraries containing compounds chemically similar to the lead compound can be generated and used to optimize the binding characteristics. These strategies have also been adopted for more detailed studies of protein-ligand interactions.

Integrity signals

Registry

Crossref · 10.1023/a:1026369729393

Cites

14 of 14 references verified0 citation errors · 0 not checkable

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  • Native MS detects ligands directly bound to a protein, whereas affinity MS approaches typically measure ligand binding indirectly as free compounds.

    “An important difference between native MS and affinity MS is that native MS detects ligands directly bound to a protein, whereas affinity MS approaches typically measure ligand binding indirectly as free compounds.”

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Authors
Kaur, S., McGuire, L., Tang, D., Dollinger, G., & Huebner, V.
Affiliations
Biochimie des Protéines Membranaires (FR)
Venue
Journal of Protein Chemistry
Published
1997-07
Volume
16
Issue
5
Pages
505-511
ISSN
  • 0277-8033 (ISSN-L)
  • 1573-4943
OpenAlex
W1226074361
Cited by
95
References
15
Citations by year
2026: 2 · 2025: 3 · 2024: 5 · 2023: 4 · 2022: 5 · 2021: 6 · 2020: 2 · 2017: 1 · 2016: 2 · 2014: 1 · 2013: 2
FWCI
5.21
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Protein Chemistry (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Keywords
affinity selection, combinatorial libraries, lead compound identification, small molecule library, protein-ligand interactions, receptor binding, drug discovery, library optimization
MeSH terms
Binding, Competitive, Chromatography, Affinity, Drug Evaluation, Preclinical, Ligands, Proteins, Receptors, Drug, Mass Spectrometry, Structure-Activity Relationship, Drug Design, Peptide Library

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