ArticleJournal of the American Society for Mass Spectrometry2011
Protein-protein binding affinities in solution determined by electrospray mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 47 citations in OpenAlex.
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- Opening opportunities for KCommunications biology · 2022Article
- Structural and mechanistic insights into amyloid-β and α-synuclein fibril formation and polyphenol inhibitor efficacy in phospholipid bilayers.The FEBS journal · 2022Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Development of hypoallergenic variants of the major horse allergen Equ c 1 for immunotherapy by rational structure based engineering.Scientific reports · 2019Article
- Conjugation of para-benzoquinone of Cigarette Smoke with Human Hemoglobin Leads to Unstable Tetramer and Reduced Cooperative Oxygen Binding.Journal of the American Society for Mass Spectrometry · 2018Article
- Ion Mobility-Mass Spectrometry Reveals Evidence of Specific Complex Formation between Human Histone Deacetylase 8 and Poly-r(C)-binding Protein 1.International journal of mass spectrometry · 2017Article
- Insight into Signal Response of Protein Ions in Native ESI-MS from the Analysis of Model Mixtures of Covalently Linked Protein Oligomers.Journal of the American Society for Mass Spectrometry · 2017Article
- 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
- Disrupting the Constitutive, Homodimeric Protein-Protein Interface in CK2β Using a Biophysical Fragment-Based Approach.Journal of the American Chemical Society · 2016Article
- Protein Structural Studies by Traveling Wave Ion Mobility Spectrometry: A Critical Look at Electrospray Sources and Calibration Issues.Journal of the American Society for Mass Spectrometry · 2016Article
- SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MS.Scientific reports · 2015Article
- Dimerization of lipocalin allergens.Scientific reports · 2015Article
- Native top-down mass spectrometry for the structural characterization of human hemoglobin.European journal of mass spectrometry (Chichester, England) · 2015Article
- An improved rapid mixing device for time-resolved electrospray mass spectrometry measurements.ChemistryOpen · 2014Article
- Cation-induced stabilization of protein complexes in the gas phase: mechanistic insights from hemoglobin dissociation studies.Journal of the American Society for Mass Spectrometry · 2014Article
- Comparative analysis of oxy-hemoglobin and aquomet-hemoglobin by hydrogen/deuterium exchange mass spectrometry.Journal of the American Society for Mass Spectrometry · 2013Article
- Staphylococcus aureus uses a novel multidomain receptor to break apart human hemoglobin and steal its heme.The Journal of biological chemistry · 2013Article
- Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry.Journal of the Royal Society, Interface · 2012Review
- Integrating mass spectrometry of intact protein complexes into structural proteomics.Proteomics · 2012Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electrospray ionization (ESI) allows the transfer of multi-protein complexes into the gas phase, thereby providing a simple approach for monitoring the stoichiometry of these noncovalent assemblies by mass spectrometry (MS). It remains unclear, however, whether the measured ion abundance ratios of free and bound species are suitable for determining solution-phase binding affinities (K(d) values). Many types of mass spectrometers employ rf-only quadrupoles as ion guides. This work demonstrates that the settings used for these devices are a key factor for ensuring uniform transmission behavior, which is a prerequisite for meaningful affinity measurements. Using bovine β-lactoglobulin and hemoglobin as model systems, it is demonstrated that under carefully adjusted conditions the "direct" ESI-MS approach is capable of providing K(d) values that are in good agreement with previously published solution-phase data. Of the several ion sources tested, a regular ESI emitter operated with pressure-driven flow at 1 μL min(-1) provided the most favorable results. Potential problems in these experiments include conformationally-induced differences in ionization efficiencies, inadvertent collision-induced dissociation, and ESI-induced clustering artifacts. A number of simple tests can be conducted to assess whether or not these factors are prevalent under the conditions used. In addition, the fidelity of the method can be scrutinized by performing measurements over a wide concentration range. Overall, this work supports the viability of the direct ESI-MS approach for determining binding affinities of protein-protein complexes in solution.
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