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Molecular characterization of sequence-driven peptide glycation.
Sci. Rep. 11:13294 (2021)
Peptide glycation is an important, yet poorly understood reaction not only found in food but also in biological systems. The enormous heterogeneity of peptides and the complexity of glycation reactions impeded large-scale analysis of peptide derived glycation products and to understand both the contributing factors and how this affects the biological activity of peptides. Analyzing time-resolved Amadori product formation, we here explored site-specific glycation for 264 peptides. Intensity profiling together with in-depth computational sequence deconvolution resolved differences in peptide glycation based on microheterogeneity and revealed particularly reactive peptide collectives. These peptides feature potentially important sequence patterns that appear in several established bio- and sensory-active peptides from independent sources, which suggests that our approach serves system-wide applicability. We generated a pattern peptide map and propose that in peptide glycation the herein identified molecular checkpoints can be used as indication of sequence reactivity.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Maillard-reaction-products; Heated Casein/sugar Solutions; End-products; Bioactive Peptides; Physicochemical Properties; Antioxidant Properties; Cross-linking; Vessel Wall; Receptor; Degradation
ISSN (print) / ISBN
2045-2322
e-ISSN
2045-2322
Journal
Scientific Reports
Quellenangaben
Volume: 11,
Issue: 1,
Article Number: 13294
Publisher
Nature Publishing Group
Publishing Place
London
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Research Unit BioGeoChemistry and Analytics (BGC)
Grants
Projekt DEAL