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Matrix-Assisted Laser Desorption Ionization-Mass Spectrometry Signal Enhancement of Peptides after Selective Extraction with Polymeric Reverse Micelles

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Abstract

Extraction of peptides by reverse micelle-forming amphiphilic homopolymers and subsequent matrix-assisted laser desorption ionization-mass spectrometry (MALDI-S) detection of these peptides in the presence of these polymers can significantly enhance peptide ion signals. Here, the mechanism of this MALDI signal enhancement is investigated. We find that the signal enhancement is caused by coalescence of polymer-peptide conjugates into "hotspots" on the MALDI target. Hotspot formation is observed only on hydrophilic surfaces and not hydrophobic surfaces. With the use of an Anchorchip MALDI target, which contains very small hydrophilic spots surrounded by a larger hydrophobic area, we find that this hotspot formation can be further exploited for ultrasensitive MALDI-MS analyses of peptides and peptide mixtures. MALDI-MS signals can be enhanced by 3-5 orders of magnitude when peptides are extracted by the amphiphilic homopolymers and detected on the Anchorchip MALDI target. This signal enhancement combined with the extraction selectivity of these reverse micelle-forming homopolymers makes these materials promising tools for sensitive detection of peptides in complex mixtures.

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