Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Optimization of guanidination procedures for MALDI mass mapping.

Richard L Beardsley1, James P Reilly

  • 1Department of Chemistry, Indiana University, Bloomington 47405, USA.

Analytical Chemistry
|May 3, 2002
PubMed
Summary

This study presents a rapid guanidination method to improve peptide detection in mass spectrometry. The procedure efficiently converts lysines to homoarginines, enhancing signal intensity for proteomics applications.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Locating Polyubiquitin Receptors on the 19S Regulatory Proteasome of <i>S. cerevisiae</i> by Cross-Linking Mass Spectrometry.

Journal of the American Society for Mass Spectrometry·2025
Same author

MEMS and ECM Sensor Technologies for Cardiorespiratory Sound Monitoring-A Comprehensive Review.

Sensors (Basel, Switzerland)·2024
Same author

Patient-centric Comparability Assessment of Biopharmaceuticals.

Journal of pharmaceutical sciences·2024
Same author

Integrated summary of immunogenicity of polatuzumab vedotin in patients with relapsed or refractory B-cell non-Hodgkin's lymphoma.

Frontiers in immunology·2023
Same author

Tracking auditory mismatch negativity responses during full conscious state and coma.

Frontiers in neurology·2023
Same author

Non-Specific Signal Peptidase Processing of Extracellular Proteins in <i>Staphylococcus aureus</i> N315.

Proteomes·2023

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Proteomics

Background:

  • Lysine derivatization is crucial for enhancing peptide detection in mass spectrometry.
  • Current guanidination methods can be time-consuming and less efficient.

Purpose of the Study:

  • To develop and optimize a rapid guanidination procedure for lysine-containing peptides.
  • To improve MALDI mass spectral signal intensities for enhanced peptide identification.
  • To evaluate the applicability of the method for low-quantity proteomics samples.

Main Methods:

  • Guanidination of lysine residues in peptides to form homoarginines.
  • Utilizing MALDI-TOF mass spectrometry for signal intensity analysis.
  • Testing the method on model peptides and tryptic protein digests.

Related Experiment Videos

  • Evaluating concentration and purification strategies for guanidinated samples.

    • Main Results:

    • Complete conversion of lysines to homoarginines achieved in as little as 5 minutes.
    • Significant increase in MALDI mass spectral signal intensities observed.
    • Successful application to 50 fmol of protein digest, demonstrating proteomics applicability.
    • Specificity of the guanidination reaction investigated using a model peptide.

    Conclusions:

    • The developed guanidination procedure offers a rapid and effective method for improving peptide detection in mass spectrometry.
    • This technique enhances the sensitivity of proteomics analyses, particularly for low-quantity samples.
    • Optimized sample preparation strategies further support the utility of this method in complex biological analyses.