Abstract
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.
Highlights
Peptide glycation is an important, yet poorly understood reaction found in food and in biological systems
It refers to a complex reaction network and produces a multitude of heterogeneous reaction products, known as Maillard reaction products (MRPs) or advanced glycation end products (AGEs)[3,4]
Most amino acids showed a wide distribution of the values, again demonstrating that the type of amino acids that contribute to Amadori product (AP) forming peptides can vary based on their immediate chemical environment. This presents a promising starting point to explore for sequencespecific glycation. To dive into this intriguing facet of peptide glycation, we examined the location of amino acids relative to the reactive peptide N-termini
Summary
Peptide glycation is an important, yet poorly understood reaction found in food and in biological systems. A limited number of studies on peptide reactivity in the MR have been conducted and focused on synthetic peptides[26,33,34] or peptide derived MRPs in specific foods[35,36,37,38] These approaches have revealed the relevance of both peptide length and composition in the MR and the importance of peptide glycation in various fields, including diverse food matrices and biological systems and disease progression[10]. We report that the combination of highresolution ESI quadrupole time of flight (QTOF) MS, bioinformatics and multivariate statistics enables a deep and molecular-level investigation of complex peptide systems Using this combinatorial method for large-scale AP analysis, we characterized the reaction behavior of 264 casein-derived peptides in the MR and used this data to gain insight into sequence-dependent differences in AP formation profiles and, peptide reactivity. This approach may be amendable to practically any type of glycation system, and it allows exploration at various levels of information, from the influence of the peptide composition to the role of specific sequence-patterns in peptide glycation
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