PLIMB: Plasma Induced Modification of Biomolecules

PLIMB is a novel and groundbreaking technology for performing hydroxyl radical protein footprinting–a technique that uses mass spectrometry to provide structure, motion, and interactions of a protein in its native state.

PLIMB leverages ionizing plasma to generate microsecond bursts of highly-reactive radicals, which covalently label solvent-accessible residues on proteins in solution.

HOw it worksRead the papers

How is PLIMB different?

How does it

PLIMB is a method to label proteins using highly reactive radicals. Our proprietary platform generates radicals quickly and labels proteins fast to ensure structural stability. The radicals rapidly label solvent-accessible residues of the protein, giving us important details about the protein's natural structure. After this process, we digest the proteins and study them using mass spectrometry. This data helps us see the differences in labeling across proteins and conditions at the single amino acid level. By assessing these labeling differences, we can learn about the structural changes in the protein under various situations, such as how it binds to an antibody or another molecule, or how it changes conformation in differing conditions.

In-solution labeling or "foot-printing"
Quench and Digestion
LC-MS/MS and Data Analysis for Identification
Peak Extraction and Quantification
Comparison of Modification Levels Between States
Dynamic structure and interactions

What the data look like

PLIMB 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.

Quantifying 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.

The proof is in the papers


Plasma-Generated OH Radical Production for Analyzing 3D Structure in Protein Therapeutics


Effect of Frequency and Applied Voltage of An Atmospheric-Pressure Dielectric-Barrier Discharge on Breakdown and Hydroxyl-Radical Generation with a Liquid Electrode