On-target and nanoparticle-facilitated selective enrichment of peptides and proteins for analysis by MALDI-MS

Authors

  • Mark L. Stolowitz

    Corresponding author
    • Canary Center at Stanford for Cancer Early Detection, Department of Radiology, Stanford University School of Medicine, Palo Alto, CA, USA
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Correspondence: Dr. Mark L. Stolowitz, Department of Radiology, Stanford University School of Medicine, 1501 California Avenue, Palo Alto, CA 94304-1110, USA

E-mail: mstolowitz@stanford.edu

Fax: +1-650-721-6921

Abstract

Over the course of the last decade, a number of investigators have come to appreciate that the surface of a MALDI target, after suitable modification, can be used for selective enrichment of peptides and proteins. More recently, surface-modified nanoparticles (NPs) that readily co-crystallize in MALDI matrix, are not ionized by laser desorption/ionization, and do not interfere with MS have attracted interest as alternatives to surface-modified targets for selective enrichment of peptides and proteins. Surface-modified targets and NPs facilitate parallel processing of samples, and when used in conjunction with MALDI mass spectrometers with kHz lasers enable development of high-throughput proteomics platforms. Targets and NPs for reversed phase and ion exchange retention, selective enrichment of glycopeptides, selective enrichment of phosphopeptides, and immunoaffinity MS are described in conjunction with details regarding their preparation and utility. Commercial availability of the reagents and substrates required to prepare surface-modified targets and NPs is also discussed.

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