Fast, high-resolution data that provides unparalleled insights into protein structure, motion and binding.
PLIMB is a novel and groundbreaking technology for performing hydroxyl radical protein footprinting–a technique which utilizes mass spectrometry to provide structural data of a protein in its native solution and conformation. PLIMB utilizes plasma to generate microsecond bursts of hydroxyl radicals, which modify and label solvent-accessible regions of a protein.
PLIMB works by labelling the proteins in solution through exposure to hydroxyl (OH) radicals. Hydroxyl radicals are highly reactive species which are generated by our proprietary plasma reactor in sub-microsecond bursts, in order to ensure structural stability during exposure. During exposure, plasma-generated radicals will label solvent-accessible side chains of the protein through a permanent covalent modification, capturing structural details of the protein in its native, in-solution state. Following exposure, proteins will then be digested and prepared for mass spectrometry analysis. Data analysis can then be used to calculate the relative abundance of modified and unmodified species on a peptide or single amino acid level. This information can then be used to assess structural differences between a protein in two distinct conditions, including bound and unbound to an antibody or ligand.
Our findings have been published in some of the most prestigious peer-reviewed journals. Your therapeutics save lives. We save you time and resources.
Crystal Structure: PLIMB technology enables precise mapping of both the epitope interactions of a therapeutic and its target, as well as allosteric conformational changes upon binding in a single experiment. Understanding the full characteristics of binding is essential to optimize the efficacy of a pharmaceutical candidate.
% Modification: By monitoring the degree of PLIMB-induced labelling on the target protein in its bound and unbound state, changes in solvent accessibility over various regions of a protein can be detected. Based on these changes, localization and characterization of the epitope interactions and allosteric conformational changes can be achieved in a simple, yet robust experimental process.
Fast, high-resolution data that provides unparalleled insights into protein structure, motion and binding.
PLIMB is a novel and groundbreaking technology for performing hydroxyl radical protein footprinting–a technique which utilizes mass spectrometry to provide structural data of a protein in its native solution and conformation. PLIMB utilizes plasma to generate microsecond bursts of hydroxyl radicals, which modify and label solvent-accessible regions of a protein.
Reduces cycle time in lead optimization by allowing rapid iteration
Reduces cost of early stage Drug Discovery Programs
Increases the number of shots on goal
Reduces risk of clinical trial failures
Allows rapid IP fillings with strong epitope claims
PLIMB works by labelling the proteins in solution through exposure to hydroxyl (OH) radicals. Hydroxyl radicals are highly reactive species which are generated by our proprietary plasma reactor in sub-microsecond bursts, in order to ensure structural stability during exposure. During exposure, plasma-generated radicals will label solvent-accessible side chains of the protein through a permanent covalent modification, capturing structural details of the protein in its native, in-solution state. Following exposure, proteins will then be digested and prepared for mass spectrometry analysis. Data analysis can then be used to calculate the relative abundance of modified and unmodified species on a peptide or single amino acid level. This information can then be used to assess structural differences between a protein in two distinct conditions, including bound and unbound to an antibody or ligand.
Our findings have been published in some of the most prestigious peer-reviewed journals. Your therapeutics save lives. We save you time and resources.
Plasma-Generated OH Radical Production for Analyzing 3D Structure
Effect of Frequency and Applied Voltage of An Atmospheric-Pressure
Crystal Structure: PLIMB technology enables precise mapping of both the epitope interactions of a therapeutic and its target, as well as allosteric conformational changes upon binding in a single experiment. Understanding the full characteristics of binding is essential to optimize the efficacy of a pharmaceutical candidate.
% Modification: By monitoring the degree of PLIMB-induced labelling on the target protein in its bound and unbound state, changes in solvent accessibility over various regions of a protein can be detected. Based on these changes, localization and characterization of the epitope interactions and allosteric conformational changes can be achieved in a simple, yet robust experimental process.