IMR Press / FBL / Volume 14 / Issue 10 / DOI: 10.2741/3482

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article

Optimization of magnetic beads for MALDI-TOF MS analysis

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1 Department of Clinical Biochemistry, Chinese PLA General Hospital, 28 Fu-Xing Road, Beijing 100853, China
2 Department of Chemistry, University of South Florida4202 E. Fowler Ave. CHE205A, Tampa, Fl 33620-5250, USA

Academic Editor: Xueji Zhang

Front. Biosci. (Landmark Ed) 2009, 14(10), 3712–3723; https://doi.org/10.2741/3482
Published: 1 January 2009
(This article belongs to the Special Issue Biosensors and their applications)
Abstract

MALDI-TOF MS is being widely applied to analyze serum samples for the diagnosis of human diseases and for the identification of potential biomarkers. However, different types of magnetic beads afford different purification capability for low abundance proteins and peptides in body fluids. The aim of our study was to establish a proteome fractionation technique for choosing magnetic beads for proteomic analysis in breast cancer research. We used three different kinds of magnetic beads (MB-HIC C8, MB-IMAC-Cu and MB-WCX) to pre-analyze 28 breast cancer patients and 24 healthy control serum samples for proteomic profiling by MALDI-TOF MS analysis. The serum samples purified by MB-WCX group provided the best proteomic pattern .These samples had the most average peak numbers, the highest peak intensities, and the best capturing ability of low abundance proteins or peptides in serum samples. Therefore, we chose MB-WCX as our best magnetic beads to pre-analyze large-scale cancer and healthy control samples. The application of the standardized, pre-analytical serum samples with right type of magnetic bead-based fractionation will decrease variability of proteome patterns in human serum assessed by MALDI-TOF MS.

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