Open AccessArticle
An Optimised Di-Boronate-ChemMatrix Affinity Chromatography to Trap Deoxyfructosylated Peptides as Biomarkers of Glycation
by
Monika Kijewska, Francesca Nuti, Magdalena Wierzbicka, Mateusz Waliczek, Patrycja Ledwoń, Agnieszka Staśkiewicz, Feliciana Real-Fernandez, Giuseppina Sabatino, Paolo Rovero, Piotr Stefanowicz, Zbigniew Szewczuk and Anna Maria Papini
Cited by 12 | Viewed by 5686
Abstract
We report herein a novel ChemMatrix
® Rink resin functionalised with two phenylboronate (PhB) moieties linked on the
N-α and
N-ε amino functions of a lysine residue to specifically capture deoxyfructosylated peptides, compared to differently glycosylated peptides in complex mixtures. The
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We report herein a novel ChemMatrix
® Rink resin functionalised with two phenylboronate (PhB) moieties linked on the
N-α and
N-ε amino functions of a lysine residue to specifically capture deoxyfructosylated peptides, compared to differently glycosylated peptides in complex mixtures. The new PhB-Lys(PhB)-ChemMatrix
® Rink resin allows for exploitation of the previously demonstrated ability of
cis diols to form phenylboronic esters. The optimised capturing and cleavage procedure from the novel functionalised resin showed that only the peptides containing deoxyfructosyl-lysine moieties can be efficiently and specifically detected by HR-MS and MS/MS experiments. We also investigated the high-selective affinity to deoxyfructosylated peptides in an ad hoc mixture containing unique synthetic non-modified peptides and in the hydrolysates of human and bovine serum albumin as complex peptide mixtures. We demonstrated that the deoxyfructopyranosyl moiety on lysine residues is crucial in the capturing reaction. Therefore, the novel specifically-designed PhB-Lys(PhB)-ChemMatrix
® Rink resin, which has the highest affinity to deoxyfructosylated peptides, is a candidate to quantitatively separate early glycation peptides from complex mixtures to investigate their role in diabetes complications in the clinics.
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