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ProteomicsIntact Transition Epitope Mapping- Thermodynamic Weak-force Order (ITEM-TWO)
Most important characteristics of antibodies are that they typically strongly bind to specific epitopes, thereby expressing low dissociation constants (KDs) and high Gibbs free binding energies (delta Gs). In this study, we describe an off-line nano-electrospray mass spectrometry method, termed IT...
ORGANISM(S): Homo sapiens (Human) 
2019-11-07 | PXD016024 | Pride
Antibody affinity determination Antibody specificity determination 
ProteomicsMass Spectrometric Analysis of Antibody-Epitope Peptide Complex Dissociation: Theoretical Concept and Practical Procedure of Binding Strength Characterization
We describe theoretical concepts and explain practical procedures of an electrospray mass spectrometry method, termed “Intact Transmission Epitope Mapping – Thermodynamic Weak-force Order (ITEM-TWO)”, by which can be determined apparent binding energies and dissociation constants of immune complex ...
ORGANISM(S): Homo sapiens (Human) Equus caballus (Horse) 
2020-10-29 | PXD021296 | Pride
Protocol Item-two Rnase s Offline esi-ms Troponin i epitope peptide-antitroponin i antibody complex Myoglobin Flag-peptide–antiflag antibody complex 
ProteomicsIntact Transition Epitope Mapping-Targeted High-Energy Rupture of Extracted Epitopes (ITEM-THREE)
ITEM-THREE is a novel mass spectrometry-based epitope mapping method. To perform ITEM-THREE, antibody-epitope peptide immune-complexes are first generated in electrospray-compatible solutions in which the antibodies maintain their in-solution functionality, by adding an antibody of interest to a mi...
ORGANISM(S): Homo sapiens (Human) 
2019-06-03 | PXD013823 | Pride
Human Molecular recognition Nanoesi Recombinant proteins Ion mobility separation Item-three Collision induced dissociation Epitope antibody complexes 
ProteomicsEpitope fine mapping by mass spectrometry: Investigations of immune complexes consisting of monoclonal anti-HpTGEKP antibody and zinc finger protein linker phospho-hexapeptides.
We describe the mass spectrometric analysis of the binding strength of a monoclonal mouse antibody (clone 18E9.D9, BioLegend, London, England) which was raised against the predominantly occuring phosphorylated linker sequence, HpTGEKP, of C2H2 zinc finger proteins (ZNF proteins) using a synthetic ...
ORGANISM(S): Homo sapiens (Human) 
2022-08-15 | PXD031150 | Pride
Item-two Off-line esi-ms Zinc finger-phosphopeptide Antiphosphopeptide-antibody Binding strength characterization 
ProteomicsIntact Transition Epitope Mapping - Force differences between Original and Unusual Residues (ITEM-FOUR)
Human cardiac Troponin I epitope peptides were incubated with monoclonal anti-cardiac Troponin I antibody. Immune complexes were subjected to nano electrospray mass spectrometry in order to determine apparent binding energies and dissociation constants of immune complex dissociation reactions in the...
ORGANISM(S): Homo sapiens (Human) 
2023-01-17 | PXD038365 | Pride
Item-four Troponin i Offline nanoesi-ms 
ProteomicsCharacterization of Phosphorylation-dependent Antibody Binding to Cancer-mutated Linkers of C2H2 Zinc Finger Proteins by Intact Transition Epitope Mapping - Thermodynamic Weak-force Order Analysis.
We describe mass spectrometric antibody-peptide binding motif analyses of a monoclonal antibody (clone 18E9.D9, BioLegend, London, England) from mouse which was raised against the predominantly occuring phosphorylated linker sequence HpTGEKP of human C2H2 zinc finger proteins. As the anti-HpTGEKP an...
ORGANISM(S): Homo sapiens (Human) 
2023-01-25 | PXD035818 | Pride
Item-two Off-line esi-ms Uterine corpus endometrial carcinoma Skin cutaneous melanoma Zinc finger-phosphopeptide Antiphosphopeptide-antibody Colon and rectal adenocarcinomas 
ProteomicsEpitope and Paratope Mapping of TNFα/Infliximab complex by cross-linking mass spectrometry and integrative modeling reveals high level of interaction specificity
Mass spectrometry (MS) has become one of the core technologies to study protein structures, protein-ligand and protein-protein interactions. Chemical cross-linking combined with mass spectrometry (XL-MS) is quickly spreading over different biochemistry laboratories for the continuous increase of its...
ORGANISM(S): Escherichia coli 
2024-02-27 | PXD043347 | Pride
Cross-linking mass spectrometry  monoclonal antibodies  integrative modeling  epitope/paratope mapping 
ProteomicsA single T cell epitope drives the neutralizing anti-drug antibody response to natalizumab in multiple sclerosis patients
Natalizumab (NZM), a humanized monoclonal IgG4 antibody to α4 integrins, is used to treat patients with relapsing-remitting multiple sclerosis (MS), but in about 6% of the cases persistent neutralizing anti-drug antibodies (ADAs) are induced leading to therapy discontinuation. To understand the basi...
ORGANISM(S): Homo sapiens (Human) 
2019-10-10 | PXD013599 | Pride
Antibody therapy Mhc-ii peptidomics Multiple sclerosis Human 
ProteomicsDetermination of protein monoclonal-antibody epitopes by a combination of structural proteomics methods.
We use a combination of multiple structural proteomics techniques (differential photo-reactive surface modification, HDX, crosslinking and epitope excision/extraction) for the determination of the protein antigen epitopes for monoclonal antibodies.
ORGANISM(S): HIV-1 M:B_MN 
2023-10-24 | PXD040902 | Pride
Hdx Limited proteolysis Surface modification Crosslinking 
UnknownBenchmark datasets of immune receptor-epitope structural complexes.
Not available
S-EPMC6785892 | biostudies-literature
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