You are here Home R & D Biologics
Mass Spectrometry

Mass Spectrometry (MS) is a popular analytical technique for determination of the elemental composition of sample or molecule. It is also used for elucidating the chemical structure of molecule, such as peptides and other chemical compounds.

We provide services for the following using the facility with two high-end Mass spectrometers Waters SYNAPT G2 HDMS as well as the AB SCIEX TripleTOF system.


Intact Mass Analysis

Molecular weight of the intact and nicked glycoproteins, organic molecules and MAbs is a key characteristic of their identity and primary structure. Mass spectrometry offers accuracy of measurement over a wide molecular weight range, with minimal, often sub-Pico mole, sample consumption. Furthermore, any difference between theoretical and measured mass may be indicative of potential modifications.

Experience and availability of wide range of mass spectrometry instruments allow us to choose the most appropriate ionization technique for the compound, from MALDI-MS, ES-MS to an LC-MS experiment for complex mixtures. At higher resolution, measurement of molecular weight to within a few ppm, often to four or five decimal places by ‘accurate mass measurement’, can aid elucidation of the elemental composition of a compound.

Peptide Mass Fingerprinting (PMF)

Peptide mass fingerprinting by mass spectrometry is used in protein characterization (primary structure evaluation) to produce a unique ‘fingerprint’ of an individual protein and to compare this with theoretical gene-derived amino acid sequence. This analysis is used for identification purposes at all stages of drug discovery or to demonstrate comparability and consistency between batches for release during manufacturing. It may also be used for the characterization of reference batches.

Peptide mapping is a very powerful tool in protein characterization and primary structure evaluation Peptide mapping is used for:

  • Disulfide bridge assignment
  • Chemical modifications
  • Impurity analysis
  • Posttranslational modifications - Glycosylation, Deamidation, Oxidation, phosphorylation etc.

Sequencing / Post-translational Modifications by MS

Mass spectrometry can be used to predict the sequencing of protein/peptides based on the masses for amino acid chains detected. This is done by subjecting the molecule to enzymatic digestion and LC-MS/MS.

This tool is useful in impurity analysis and detecting posttranslational modifications like glycosylation, deamidation, oxidation, phosphorylation etc. in a protein/peptide and can provide in-depth understand of the different forms of a molecule present in a product.