MALDIPepQuant

MALDIPepQuant quantifies peptides from Matrix-Assisted Laser Desorption/Ionization (MALDI) mass spectrometry using Stable Isotope Labeling by Amino acids in Cell culture (SILAC) to measure relative protein expression.


Key Features:

  • Integration with SILAC: Implements SILAC-based peptide quantification by comparing labeled and unlabeled peptides.
  • Compatibility with Phenyx output: Processes mass spectrometry data output from Phenyx for MALDI peptide quantification.
  • Leucine labeling and sensitivity: Employs replacement of natural leucine with [(13)C6]leucine in a semidefined medium to enable quantification and detect at least 50% variation in protein expression.

Scientific Applications:

  • Quantitative proteomics: Enables relative quantification of protein expression levels in proteomic studies.
  • Microbial proteomics: Applied to organisms such as Bifidobacterium longum for peptide-level quantification.
  • Biological investigations: Suitable for studies of cellular responses, disease mechanisms, and metabolic pathways that require peptide quantification.

Methodology:

Uses SILAC by replacing natural leucine with [(13)C6]leucine in a semidefined medium, differentiates labeled and unlabeled peptides during MALDI analysis, and quantifies peptides by analyzing Phenyx mass spectrometry output.

Topics

Collections

Details

Tool Type:
web application
Operating Systems:
Linux, Windows, Mac
Programming Languages:
Java
Added:
12/6/2017
Last Updated:
9/4/2019

Operations

Publications

Couté Y, Hernandez C, Appel RD, Sanchez J, Margolles A. Labeling of <i>Bifidobacterium longum</i> Cells with <sup>13</sup> C-Substituted Leucine for Quantitative Proteomic Analyses. Applied and Environmental Microbiology. 2007;73(17):5653-5656. doi:10.1128/aem.00667-07. PMID:17601805. PMCID:PMC2042066.

Documentation