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Issue 23, 2012
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Affinity surface-assisted laser desorption/ionization mass spectrometry for peptide enrichment

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Abstract

In this paper, we report on the functionalization of silicon nanostructured (NanoSi) surface with an organic layer of nitrilotriacetic acid (NTA) and its subsequent use as an affinity surface-assisted laser desorption/ionization mass spectrometry (SALDI-MS) interface for histidine-tagged peptide enrichment and mass spectrometry analysis. The NTA terminal groups are immobilized onto the NanoSi surface via very stable Si–C covalent bonds. The NTA-modified NanoSi (NTA-NanoSi) interface was characterized by contact angle measurements, Fourier transform infrared (FTIR) spectroscopy and X-ray photoelectron spectroscopy (XPS). The NTA-NanoSi interface has shown a good selectivity toward His-tagged peptide and permits its enrichment from an artificial mixture of both tagged and untagged peptides and its subsequent mass spectrometry detection with good signal/noise ratio.

Graphical abstract: Affinity surface-assisted laser desorption/ionization mass spectrometry for peptide enrichment

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Supplementary files

Article information


Submitted
15 Jun 2012
Accepted
22 Sep 2012
First published
25 Sep 2012

Analyst, 2012,137, 5527-5532
Article type
Paper

Affinity surface-assisted laser desorption/ionization mass spectrometry for peptide enrichment

Y. Coffinier, N. Nguyen, H. Drobecq, O. Melnyk, V. Thomy and R. Boukherroub, Analyst, 2012, 137, 5527 DOI: 10.1039/C2AN35803D

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