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Peptide Identification Using Tandem Mass Spectrometry

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

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Peptide and Protein Quantification Using Automated Immuno-MALDI iMALDI

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Published on: August 18, 2017

Development of MALDI MS peptide array for thrombin inhibitor screening.

Weiwei Tang¹, Andrew Gordon¹, Hui-Ying Wang¹

¹State Key Laboratory of Natural Medicines and School of Traditional Chinese Pharmacy, China Pharmaceutical University, Nanjing, 210009, China.

|March 7, 2021

Summary

A new peptide array on indium tin oxide slides enables in situ analysis of thrombin activity. This method successfully identified potent natural thrombin inhibitors from grape seed proanthocyanidins.

Keywords:

Enzyme assay Inhibitor screening Mass spectrometry imaging Proanthocyanidins Surface-based MS

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Last Updated: Nov 15, 2025

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Identifying Protein-protein Interaction Sites Using Peptide Arrays

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Area of Science:

Biochemistry
Analytical Chemistry
Drug Discovery

Background:

Enzyme activity analysis is crucial for drug discovery and development.
In situ methods offer advantages for real-time monitoring and visualization.
Thrombin plays a key role in various physiological and pathological processes.

Purpose of the Study:

To develop a novel peptide array for in situ analysis and visualization of enzyme activity.
To investigate thrombin activity and screen for its inhibitors using the developed platform.
To assess the anti-thrombin activity of grape seed proanthocyanidins.

Main Methods:

Fabrication of functionalized indium tin oxide (ITO) glass slides with immobilized peptides.
Non-covalent immobilization of phospholipid-tagged peptides on steric acid-modified ITO slides.
Utilizing matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS) for peptide array analysis and imaging.

Main Results:

The developed peptide arrays are compatible with MALDI MS, free of matrix peak interference, and tolerate aqueous washing.
Thrombin activity and Michaelis-Menten constant (K_m) for the immobilized substrate were determined.
Grape seed proanthocyanidins with a mean degree of polymerization (DP) of 4.61-6.82 exhibited significant anti-thrombin activity (IC₅₀ < 10 μg/mL).

Conclusions:

The developed peptide array serves as a reliable platform for in situ enzyme activity analysis and inhibitor screening.
This method facilitates the discovery of natural products, such as grape seed proanthocyanidins, as potential therapeutic agents.
The platform enables visualization of enzyme activity and inhibitor effects, aiding in drug discovery research.