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Updated: Aug 30, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
Published on: October 15, 2018
Analysis of self-assembled monolayer interfaces by electrospray mass spectrometry: a gentle approach
Wenrong Yang1, Rui Zhang, Gary D Willett
1School of Chemical Sciences, The University of New South Wales, Sydney, NSW 2052, Australia.
Abstract:
A general mass spectrometry technique for the characterization of alkanethiol-modified surfaces is presented. Alkanethiol self-assembled onto a gold surface (in this case, peptides were attached to the gold surface via a thiolate bond) was reductively desorbed in 0.05 M KOH in the presence of octadecyl-derivatized silica gel. The peptide adsorbed onto the silica gel, whereupon it could be filtered, washed to remove any salts, and then eluted using a mixture of 4:1 v/v methanol/water. The eluant containing the peptide was injected into a Fourier transform ion-cyclotron resonance mass spectrometer (FTICR/MS) via electrospray ionization. The spectrum showed no fragmentation of the peptide, demonstrating the gentleness of the technique. This simple procedure is not limited to FTICR/MS and could be adapted to other mass spectrometers.
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