ArticleJournal of the American Society for Mass Spectrometry2016
Optimization of Electrospray Ionization by Statistical Design of Experiments and Response Surface Methodology: Protein-Ligand Equilibrium Dissociation Constant Determinations.
Article in Journal of the American Society for Mass Spectrometry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
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- Species-specific optimization of oxylipin ionization in LC-MS: a design of experiments approach to improve sensitivity.Analytical and bioanalytical chemistry · 2025Article
- Determination of Binding Constants and Gas Phase Stabilities of Artificial Carbohydrate Receptor Complexes Using Electrospray Mass Spectrometry.ACS omega · 2024Article
- Natural Product Graveoline Modulates Kirsten Rat Sarcoma Viral Oncogene Homologue (KRAS) Membrane Association: Insights from Advanced Spectroscopic Studies.ACS pharmacology & translational science · 2024Article
- Development of a sensitive LC-MS/MS assay to support human microdose study for an oral agonist of the GLP-1 receptor.Bioanalysis · 2024Article
- Kinetics of ligand exchange in solution: a quantitative mass spectrometry approach.Chemical science · 2023Article
- Drug-Repurposing Screening Identifies a Gallic Acid Binding Site on SARS-CoV-2 Non-structural Protein 7.ACS pharmacology & translational science · 2023Article
- Collision-Induced Affinity Selection Mass Spectrometry for Identification of Ligands.ACS bio & med chem Au · 2022Article
- Quantifying Biomolecular Interactions Using Slow Mixing Mode (SLOMO) Nanoflow ESI-MS.ACS central science · 2022Article
- Towards Unbiased Evaluation of Ionization Performance in LC-HRMS Metabolomics Method Development.Metabolites · 2022Article
- Efficient discovery of potential inhibitors for SARS-CoV-2 3C-like protease from herbal extracts using a native MS-based affinity-selection method.Journal of pharmaceutical and biomedical analysis · 2022Article
- Challenges and stepwise fit-for-purpose optimization for bioanalyses of remdesivir metabolites nucleotide monophosphate and triphosphate in mouse tissues using LC-MS/MS.Journal of pharmaceutical and biomedical analysis · 2021Article
- Development of a target identification approach using native mass spectrometry.Scientific reports · 2021Article
- Development and Optimization of a High Sensitivity LC-MS/MS Method for the Determination of Hesperidin and Naringenin in Rat Plasma: Pharmacokinetic Approach.Molecules (Basel, Switzerland) · 2020Article
- Anti-SARS-CoV-2 activities in vitro of Shuanghuanglian preparations and bioactive ingredients.Acta pharmacologica Sinica · 2020Article
- Discovery of a Natural Product That Binds to theMolecules (Basel, Switzerland) · 2020Article
- A Phenotarget Approach for Identifying an Alkaloid Interacting with the Tuberculosis Protein Rv1466.Marine drugs · 2020Article
- Review
- Fragment-Based Screening of a Natural Product Library against 62 Potential Malaria Drug Targets Employing Native Mass Spectrometry.ACS infectious diseases · 2018Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electrospray ionization mass spectrometry (ESI-MS) binding studies between proteins and ligands under native conditions require that instrumental ESI source conditions are optimized if relative solution-phase equilibrium concentrations between the protein-ligand complex and free protein are to be retained. Instrumental ESI source conditions that simultaneously maximize the relative ionization efficiency of the protein-ligand complex over free protein and minimize the protein-ligand complex dissociation during the ESI process and the transfer from atmospheric pressure to vacuum are generally specific for each protein-ligand system and should be established when an accurate equilibrium dissociation constant (KD) is to be determined via titration. In this paper, a straightforward and systematic approach for ESI source optimization is presented. The method uses statistical design of experiments (DOE) in conjunction with response surface methodology (RSM) and is demonstrated for the complexes between Plasmodium vivax guanylate kinase (PvGK) and two ligands: 5'-guanosine monophosphate (GMP) and 5'-guanosine diphosphate (GDP). It was verified that even though the ligands are structurally similar, the most appropriate ESI conditions for KD determination by titration are different for each. Graphical Abstract ᅟ.
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