ArticleBiophysics and physicobiology2016
Mass spectrometric analysis of protein-ligand interactions.
Article in Biophysics and physicobiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 44 citations in OpenAlex.
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- Food Antioxidants and Their Interaction with Human Proteins.Antioxidants (Basel, Switzerland) · 2023Review
- Collision-Induced Affinity Selection Mass Spectrometry for Identification of Ligands.ACS bio & med chem Au · 2022Article
- Structural Characterization of Carbonic Anhydrase-Arylsulfonamide Complexes Using Ultraviolet Photodissociation Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2021Article
- Development of a target identification approach using native mass spectrometry.Scientific reports · 2021Article
- Microscale thermophoresis as a powerful tool for screening glycosyltransferases involved in cell wall biosynthesis.Plant methods · 2020Article
- Mass spectrometry-based analysis of macromolecular complexes ofFEBS open bio · 2019Article
- Revealing the architecture of protein complexes by an orthogonal approach combining HDXMS, CXMS, and disulfide trapping.Nature protocols · 2018Article
- RecA requires two molecules of Mg2+ ions for its optimal strand exchange activity in vitro.Nucleic acids research · 2018Article
- Preliminary investigation of deoxyoligonucleotide binding to ribonuclease A using mass spectrometry: An attempt to develop a lab experience for undergraduates.F1000Research · 2018Article
- Preface of Special Issue "Protein-Ligand Interactions".Biophysics and physicobiology · 2016Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interactions of small molecules with proteins (protein-ligand interactions) mediate various biological phenomena including signal transduction and protein transcription and translation. Synthetic compounds such as drugs can also bind to target proteins, leading to the inhibition of protein-ligand interactions. These interactions typically accompany association-dissociation equilibrium according to the free energy difference between free and bound states; therefore, the quantitative biophysical analysis of the interactions, which uncovers the stoichiometry and dissociation constant, is important for understanding biological reactions as well as for rational drug development. Mass spectrometry (MS) has been used to determine the precise molecular masses of molecules. Recent advancements in MS enable us to determine the molecular masses of protein-ligand complexes without disrupting the non-covalent interactions through the gentle desolvation of the complexes by increasing the vacuum pressure of a chamber in a mass spectrometer. This method is called MS under non-denaturing conditions or native MS and allows the unambiguous determination of protein-ligand interactions. Under a few assumptions, MS has also been applied to determine the dissociation constants for protein-ligand interactions. The structural information of a protein-ligand interaction, such as the location of the interaction and conformational change in a protein, can also be analyzed using hydrogen/deuterium exchange MS. In this paper, we briefly describe the history, principle, and recent applications of MS for the study of protein-ligand interactions.
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