Leveraging breakthrough technologies to map linear, conformational and discontinuous epitopes with amino acid level resolution
a revolutionary technology that generates free radicals from a plasma for Protein Footprinting. PLIMB is used for analyzing protein structure and interactions with unprecedented degree of speed, resolution and accuracy.
PLIMB is a revolutionary technique that provides high resolution data on the native, in-solution structure of the therapeutic and target antigen in a rapid analysis that is applicable to a wide range of proteins.
Epitope Mapping of HER2 with Single Amino Acid-Level Resolution using a Combination of Plasma-Initiated CF3 and Hydroxyl Radical Footprinting
PLIMB Nature Science Report 2017
Epitope Mapping of Antithrombin mAB by PLIMB
Developed in 2002, Hydroxyl Radical Protein Footprinting (HRF) has a long track record of success in academic labs for protein structural studies. At Immuto Scientific, we are leveraging this powerful, highly validated technique to analyze protein-protein interactions and map epitopes with an unprecedented degree of speed, resolution and accuracy.
Selected Publications:
Plasma-Generated OH Radical Production for Analyzing Three-Dimensional Structure in Protein Therapeutics
Epitope mapping of anti-drug antibodies to a clinical candidate bispecific antibody
Antigen physiochemical properties allosterically effect the IgG Fc-region and Fc neonatal receptor affinity
Antibody-receptor interactions mediate antibody-dependent cellular cytotoxicity
High-Resolution Hydroxyl Radical Protein Footprinting: Biophysics Tool for Drug Discovery
Current Trends in Biotherapeutic Higher Order Structure Characterization by Irreversible Covalent Footprinting Mass Spectrometry
Hydroxyl radical protein footprinting for analysis of higher order structure
Protein Footprinting Comes of Age: Mass Spectrometry for Biophysical Structure Assessment
Characterization of ELISA Antibody-Antigen Interaction using Footprinting-Mass Spectrometry and Negative Staining Transmission Electron Microscopy
Hydroxyl Radical Protein Footprinting: A Mass Spectrometry-Based Structural Method for Studying the Higher Order Structure of Proteins
High Structural Resolution Hydroxyl Radical Protein Footprinting Reveals an Extended Robo1-Heparin Binding Interface
Conformational Analysis of Therapeutic Proteins by Hydroxyl Radical Protein Footprinting
Hydroxyl radical-mediated modification of proteins as probes for structural proteomics
Covalent Labeling Techniques for Characterizing Higher Order Structure of Monoclonal Antibodies
Quantitative protein topography analysis and high- resolution structure prediction using hydroxyl radical labeling and tandem-ion mass spectrometry (MS)
Quantitative mapping of protein structure by hydroxyl radical footprinting-mediated structural mass spectrometry: a protection factor analysis
Protein Footprinting: Auxiliary Engine to Power the Structural Biology Revolution.
Hydroxyl Radical Protein Footprinting: A Mass Spectrometry-Based Structural Method for Studying the Higher Order Structure of Proteins
We are leveraging breakthrough technologies to transform drug discovery.
Acquiring detailed knowledge of epitope interactions is critical in the lead validation stage of drug discovery, as it provides insight into the binding mechanism, enabling the optimization of various properties of a drug candidate such as specificity and binding affinity.
Furthermore, a detailed epitope map can provide stronger intellectual property (IP) protection. Epitope claims included in drug patents protect against binders to a specific epitope of the given target, allowing for much broader IP protection.
PLIMB is a revolutionary technique that provides high resolution data on the native, in-solution structure of the therapeutic and target antigen in a rapid analysis that is applicable to a wide range of proteins.
