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Proteome Sci. 2011 Oct 14;9 Suppl 1:S10. doi: 10.1186/1477-5956-9-S1-S10.

A new method for alignment of LC-MALDI-TOF data.

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1
Lombardi Comprehensive Cancer Center, Georgetown University, Washington, DC, USA. hwr@georgetown.edu.

Abstract

BACKGROUND:

In proteomics studies, liquid chromatography coupled to mass spectrometry (LC-MS) has proven to be a powerful technology to investigate differential expression of proteins/peptides that are characterized by their peak intensities, mass-to-charge ratio (m/z), and retention time (RT). The variable complexity of peptide mixtures and occasional drifts lead to substantial variations in m/z and RT dimensions. Thus, label-free differential protein expression studies by LC-MS technology require alignment with respect to both RT and m/z to ensure that same proteins/peptides are compared from multiple runs.

METHODS:

In this study, we propose a new strategy to align LC-MALDI-TOF data by combining quality threshold cluster analysis and support vector regression. Our method performs alignment on the basis of measurements in three dimensions (RT, m/z, intensity).

RESULTS AND CONCLUSIONS:

We demonstrate the suitability of our proposed method for alignment of LC-MALDI-TOF data through a previously published spike-in dataset and a new in-house generated spike-in dataset. A comparison of our method with other methods that utilize only RT and m/z dimensions reveals that the use of intensity measurements enhances alignment performance.

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