What Is Mass Spectrometry?

Mass spectrometry (MS) is an analytical technique that measures the mass-to-charge ratio of ionized molecules. By converting compounds into charged particles and separating them in an analyzer, MS allows researchers to determine molecular weights, identify unknown compounds, and analyze complex mixtures with high sensitivity.

(Reference: Aebersold & Mann, 2003)

Why Use MS in Peptide Research?

Peptides are small chains of amino acids that can vary in sequence, modifications, and purity. Mass spectrometry has become an essential tool for their study because it provides precise molecular information. Researchers use MS to:

• Confirm peptide identity by measuring exact molecular weight.

• Detect post-translational or synthetic modifications.

• Assess purity and identify by-products in synthetic preparations.

• Sequence peptides through fragmentation analysis.

(Reference: Yates et al., 2009)

Common Approaches in Peptide MS

Several methods are frequently applied in peptide analysis:

• MALDI-TOF (Matrix-Assisted Laser Desorption/Ionization–Time of Flight) – Often used for rapid mass determination of peptides.

• ESI (Electrospray Ionization) – Allows analysis of peptides in solution, suitable for coupling with liquid chromatography.

• LC-MS/MS (Liquid Chromatography–Tandem Mass Spectrometry) – Combines separation with fragmentation for detailed sequencing and structural analysis.

(Reference: Domon & Aebersold, 2006)

Research Applications

Mass spectrometry is widely used in peptide science, including:

• Verifying synthetic peptide batches for identity and purity.

• Mapping peptide–protein interactions.

• Profiling endogenous peptides in biological samples.

• Supporting structural studies by pinpointing amino acid modifications.

(Reference: Aebersold & Mann, 2016)

References

• Aebersold, R., & Mann, M. (2003). Mass spectrometry-based proteomics. Nature, 422, 198–207.

• Yates, J.R., et al. (2009). Proteomics by mass spectrometry: approaches, advances, and applications. Annual Review of Biochemistry, 78, 243–272.

• Domon, B., & Aebersold, R. (2006). Mass spectrometry and protein analysis. Science, 312(5771), 212–217.

• Aebersold, R., & Mann, M. (2016). Mass-spectrometric exploration of proteome structure and function. Nature, 537, 347–355.

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