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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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Monitoring Protein Adsorption with Solid-state Nanopores

Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

Single Molecule Nanopore Spectrometry for Peptide Detection.

Amy E Chavis¹, Kyle T Brady¹, Grace A Hatmaker¹

¹Department of Physics, Virginia Commonwealth University , Richmond, Virginia 23284, United States.

|August 17, 2017

Summary

Single molecule nanopore spectrometry (SMNS) now effectively senses water-soluble peptides. Enhancements improve peptide detection and mass resolution, crucial for bioapplications.

Keywords:

Au25(SG)18 alpha hemolysin angiotensin nanomolecules neurotensin peptides resistive-pulse nanopore sensing thiolate-capped clusters

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Published on: July 16, 2018

Area of Science:

Biophysics
Analytical Chemistry
Materials Science

Background:

Single molecule nanopore spectrometry (SMNS) offers potential for molecular size discrimination.
Previous studies demonstrated SMNS for differentiating polyethylene glycol (PEG) molecules.
Extending SMNS to water-soluble peptides is vital for various bioapplications.

Purpose of the Study:

To enhance single molecule nanopore spectrometry (SMNS) for sensing water-soluble peptides.
To investigate the impact of Au25(SG)18 clusters on peptide-nanopore interactions.
To analyze the role of fluctuations and solution conditions in peptide detection.

Main Methods:

Utilized Au25(SG)18 clusters to modulate peptide on- and off-rates to the nanopore.
Investigated the effect of solution conditions (pH, chaotropic salt) on peptide flexibility and current blockade fluctuations.
Developed a model correlating current blockade depths to peptide mass.

Main Results:

Au25(SG)18 clusters were employed to enhance peptide binding kinetics.
Increased peptide flexibility via solution modification reduced current blockade fluctuations by nearly 2-fold.
Enhanced SMNS improved mass resolution by over 2-fold for cationic peptides.

Conclusions:

Optimized SMNS, incorporating Au25(SG)18 clusters and controlled solution conditions, significantly improves water-soluble peptide sensing.
The study provides a model linking peptide mass to current blockade depth, enhancing sensor accuracy.
These advancements are critical for advancing bioanalytical applications relying on peptide characterization.