Molecular characterization of sequence-driven peptide glycation

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...

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Autores principales:	Michelle T. Berger, Daniel Hemmler, Alesia Walker, Michael Rychlik, James W. Marshall, Philippe Schmitt-Kopplin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fbe7acb3b809413195d82d144779ff59
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spelling	oai:doaj.org-article:fbe7acb3b809413195d82d144779ff592021-12-02T17:45:03ZMolecular characterization of sequence-driven peptide glycation10.1038/s41598-021-92413-72045-2322https://doaj.org/article/fbe7acb3b809413195d82d144779ff592021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-92413-7https://doaj.org/toc/2045-2322Abstract 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.Michelle T. BergerDaniel HemmlerAlesia WalkerMichael RychlikJames W. MarshallPhilippe Schmitt-KopplinNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Michelle T. Berger Daniel Hemmler Alesia Walker Michael Rychlik James W. Marshall Philippe Schmitt-Kopplin Molecular characterization of sequence-driven peptide glycation
description	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.
format	article
author	Michelle T. Berger Daniel Hemmler Alesia Walker Michael Rychlik James W. Marshall Philippe Schmitt-Kopplin
author_facet	Michelle T. Berger Daniel Hemmler Alesia Walker Michael Rychlik James W. Marshall Philippe Schmitt-Kopplin
author_sort	Michelle T. Berger
title	Molecular characterization of sequence-driven peptide glycation
title_short	Molecular characterization of sequence-driven peptide glycation
title_full	Molecular characterization of sequence-driven peptide glycation
title_fullStr	Molecular characterization of sequence-driven peptide glycation
title_full_unstemmed	Molecular characterization of sequence-driven peptide glycation
title_sort	molecular characterization of sequence-driven peptide glycation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/fbe7acb3b809413195d82d144779ff59
work_keys_str_mv	AT michelletberger molecularcharacterizationofsequencedrivenpeptideglycation AT danielhemmler molecularcharacterizationofsequencedrivenpeptideglycation AT alesiawalker molecularcharacterizationofsequencedrivenpeptideglycation AT michaelrychlik molecularcharacterizationofsequencedrivenpeptideglycation AT jameswmarshall molecularcharacterizationofsequencedrivenpeptideglycation AT philippeschmittkopplin molecularcharacterizationofsequencedrivenpeptideglycation
_version_	1718379624237367296

Molecular characterization of sequence-driven peptide glycation

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