One-step maltose-functionalization of magnetic nanoparticles based on self-assembled oligopeptides for selective enrichment of glycopeptides

Abstract Magnetic nanoparticles (MNPs) have been widely explored in enrichment of low-abundance glycoproteins/glycopeptides prior to mass spectrometry analysis in glycoproteomics. Currently, most functional groups for recognizing glycoproteins/glycopeptides are usually immobilized on the nanomaterial surface based on covalent modification, which suffers from multistep treatment, surface-dependence, and harsh conditions. In this work, we first report a facile and rapid method for surface functionalization and subsequent glycopeptides enrichment via one-step assembly of maltose-modified oligopeptides with a sequence of Ala-Glu-Ala-Glu-Ala-Lys-Ala-Lys (AEK8-maltose). In physiological conditions, AEK8-maltose readily self-organized into a complete coating layer dominated by β-sheets on the surface of SiO2@Fe3O4 and C@Fe3O4 MNPs, which remain intact to repeat washing with acidic organic and aqueous solutions extensively used in the sample enrichment treatments. Thus, the resulting AEK8-maltose functionalized MNPs show excellent performance in enrichment of glycopeptides in standard glycoprotein digests (24 glycopeptides from horseradish peroxidase (HRP), 31 glycopeptides from immunoglobulin (IgG)) and human serum digests (282 glycopeptides), including rapid enrichment speed (5 min), high detection sensitivity (0.001 ng/μL HRP), high selectivity (mass ratios of HRP and bovine serum albumin (BSA) digests up to 1:150), good enrichment recovery (over 86.3%), remarkable stability (repeatable for more than 8 times), and excellent renewability, which are better than or comparable with the literature results reported to date. The current work based on self-assembling oligopeptides provides a mild, economic and nontoxic procedure for one-step surface functionalization of various nanomaterials.