{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lux S"],"funding":["European Fund for Regional and Structure Development (EFRE)","European Fund for Regional and Structure Development","Universität Leipzig"],"pagination":["5239-5251"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12431902"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["417(23)"],"pubmed_abstract":["Protein glycation, or non-enzymatic glycosylation, refers to the reaction of reducing sugars with amino groups in proteins to form Amadori and Heyns products for aldoses (e.g., glucose) and ketoses (e.g., fructose), respectively. While Amadori peptides have been well studied after enrichment by boronate affinity chromatography (BAC), it is often assumed that BAC also enriches the isomeric Heyns peptides, although the binding of Heyns rearrangement products seems unlikely due to the very low content of 1,2- and 1,3-cis-diols in their dominant tautomeric forms. For seven different tryptic peptide sequences derived from human plasma digests, we showed that the synthetic glucose-modified Amadori peptides can be enriched by BAC with high recovery rates, while the corresponding fructose-modified"],"journal":["Analytical and bioanalytical chemistry"],"pubmed_title":["Limitations of boronate affinity chromatography for the specific enrichment of fructose-derived early glycation products in protein analytics."],"pmcid":["PMC12431902"],"funding_grant_id":["100689097"],"pubmed_authors":["Vogt C","Lux S","Voll M","Hoffmann R"],"additional_accession":[]},"is_claimable":false,"name":"Limitations of boronate affinity chromatography for the specific enrichment of fructose-derived early glycation products in protein analytics.","description":"Protein glycation, or non-enzymatic glycosylation, refers to the reaction of reducing sugars with amino groups in proteins to form Amadori and Heyns products for aldoses (e.g., glucose) and ketoses (e.g., fructose), respectively. While Amadori peptides have been well studied after enrichment by boronate affinity chromatography (BAC), it is often assumed that BAC also enriches the isomeric Heyns peptides, although the binding of Heyns rearrangement products seems unlikely due to the very low content of 1,2- and 1,3-cis-diols in their dominant tautomeric forms. For seven different tryptic peptide sequences derived from human plasma digests, we showed that the synthetic glucose-modified Amadori peptides can be enriched by BAC with high recovery rates, while the corresponding fructose-modified","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-06-03T02:51:56.998Z","creation":"2026-04-23T03:12:12.746Z"},"accession":"S-EPMC12431902","cross_references":{"pubmed":["40770571"],"doi":["10.1007/s00216-025-06044-2"]}}