ArticleJournal of the American Society for Mass Spectrometry2012
Quantifying protein-ligand binding constants using electrospray ionization mass spectrometry: a systematic binding affinity study of a series of hydrophobically modified trypsin inhibitors.
Article in Journal of the American Society for Mass Spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed.
- Quantifying Protein Homodimer Affinities and the Effect of Molecular Glues and Interface Residues Using Native Mass Spectrometry.Journal of the American Chemical Society · 2026Article
- Structural mass spectrometry techniques for characterisation of plant and algal proteins.The Plant journal : for cell and molecular biology · 2026Review
- Optimization of galectin-3 binding agents by in situ multiple compound synthesis and native mass spectrometry.Scientific reports · 2026Article
- Characterization of two orthologs of bacterial intramembrane metalloprotease RseP by native mass spectrometry.Analytical and bioanalytical chemistry · 2025Article
- Allostery without Conformational Change: A Native Mass Spectrometry Perspective.The journal of physical chemistry. B · 2025Article
- Considerations for defining +80 Da mass shifts in mass spectrometry-based proteomics: phosphorylation and beyond.Chemical communications (Cambridge, England) · 2023Review
- Quantitative Characterization of Three Carbonic Anhydrase Inhibitors by LESA Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
- Exploring the Conformational Landscape and Stability of Aurora A Using Ion-Mobility Mass Spectrometry and Molecular Modeling.Journal of the American Society for Mass Spectrometry · 2022Article
- Discovering protein-protein interaction stabilisers by native mass spectrometry.Chemical science · 2021Article
- DNA Binding and Phosphorylation Regulate the Core Structure of the NF-κB p50 Transcription Factor.Journal of the American Society for Mass Spectrometry · 2019Article
- An Electrospray Ionization Mass Spectrometry Study on the "In Vacuo" Hetero-Oligomers Formed by the Antimicrobial Peptides, Surfactin and Gramicidin S.Journal of the American Society for Mass Spectrometry · 2017Article
- Cis→Trans Isomerization of Pro(7) in Oxytocin Regulates Zn(2+) Binding.Journal of the American Society for Mass Spectrometry · 2016Article
- Origin and prediction of free-solution interaction studies performed label-free.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Influence of Sulfolane on ESI-MS Measurements of Protein-Ligand Affinities.Journal of the American Society for Mass Spectrometry · 2016Article
- Probing allosteric mechanisms using native mass spectrometry.Current opinion in structural biology · 2015Review
- An improved rapid mixing device for time-resolved electrospray mass spectrometry measurements.ChemistryOpen · 2014Article
- Extracting structural information from charge-state distributions of intrinsically disordered proteins by non-denaturing electrospray-ionization mass spectrometry.Intrinsically disordered proteinsReview
Corrections and comments
- Erratum issued
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NanoESI-MS is used for determining binding strengths of trypsin in complex with two different series of five congeneric inhibitors, whose binding affinity in solution depends on the size of the P3 substituent. The ligands of the first series contain a 4-amidinobenzylamide as P1 residue, and form a tight complex with trypsin. The inhibitors of the second series have a 2-aminomethyl-5-chloro-benzylamide as P1 group, and represent a model system for weak binders. The five different inhibitors of each group are based on the same scaffold and differ only in the length of the hydrophobic side chain of their P3 residue, which modulates the interactions in the S3/4 binding pocket of trypsin. The dissociation constants (K(D)) for high affinity ligands investigated by nanoESI-MS ranges from 15 nM to 450 nM and decreases with larger hydrophobic P3 side chains. Collision-induced dissociation (CID) experiments of five trypsin and benzamidine-based complexes show a correlation between trends in K(D) and gas-phase stability. For the second inhibitor series we could show that the effect of imidazole, a small stabilizing additive, can avoid the dissociation of the complex ions and as a result increases the relative abundance of weakly bound complexes. Here the K(D) values ranging from 2.9 to 17.6 μM, some 1-2 orders of magnitude lower than the first series. For both ligand series, the dissociation constants (K(D)) measured via nanoESI-MS were compared with kinetic inhibition constants (K(i)) in solution.
Indexed as
Identifiers
22869298What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.