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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

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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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MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

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Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
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Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

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Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
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Related Experiment Video

Updated: Apr 6, 2026

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide
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Study of CPP Mechanisms by Mass Spectrometry.

Sandrine Sagan1, Chérine Bechara, Fabienne Burlina

  • 1Sorbonne Universités, UPMC Univ Paris 06 LBM, Paris, France.

Methods in Molecular Biology (Clifton, N.J.)
|July 24, 2015
PubMed
Summary

Researchers developed a new method using mass spectrometry to precisely measure how much of cell-penetrating peptides (CPPs) enter cells and how they break down inside. This technique aids in studying CPPs

Area of Science:

  • Biochemistry and Molecular Biology
  • Cell Biology
  • Analytical Chemistry

Background:

  • Cell-penetrating peptides (CPPs) are crucial for delivering molecules into cells.
  • Accurate methods are needed to quantify CPP uptake, stability, and localization.
  • Existing methods may have limitations in sensitivity or scope.

Purpose of the Study:

  • To introduce a novel protocol for the direct detection and quantification of internalized cell-penetrating peptides (CPPs).
  • To enable the analysis of metabolic stability and intracellular degradation of CPPs.
  • To facilitate the simultaneous analysis of multiple CPP species.

Main Methods:

  • Direct detection of peptides using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).

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  • Absolute quantification of intact internalized CPPs.
  • Analysis of intracellular peptide degradation products.

    • Main Results:

    • The developed MALDI-TOF MS protocol allows for the absolute quantification of intact internalized CPPs.
    • The method enables the monitoring of intracellular degradation pathways of CPPs.
    • The protocol is adaptable for simultaneous quantification of CPP mixtures.

    Conclusions:

    • This MALDI-TOF MS-based protocol provides a reliable and sensitive method for studying CPP cellular entry mechanisms.
    • The technique enhances the understanding of CPP pharmacokinetics and intracellular fate.
    • It offers a versatile tool for researchers investigating CPPs and related drug delivery systems.