Synergistic sequence contributions bias glycation outcomes

Advanced glycation end-products (AGEs), such as methylglyoxal-derived hydroimidazolone isomer (MGH-1), are associated with disease and age-related disorders, and occur spontaneously, so it is unclear why specific protein sites become modified with specific AGEs. Here, the authors use a combinatorial...

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Autores principales:	Joseph M. McEwen, Sasha Fraser, Alexxandra L. Sosa Guir, Jaydev Dave, Rebecca A. Scheck
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5fba806714964ba4b997f252adebc342
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spelling	oai:doaj.org-article:5fba806714964ba4b997f252adebc3422021-12-02T18:24:49ZSynergistic sequence contributions bias glycation outcomes10.1038/s41467-021-23625-82041-1723https://doaj.org/article/5fba806714964ba4b997f252adebc3422021-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23625-8https://doaj.org/toc/2041-1723Advanced glycation end-products (AGEs), such as methylglyoxal-derived hydroimidazolone isomer (MGH-1), are associated with disease and age-related disorders, and occur spontaneously, so it is unclear why specific protein sites become modified with specific AGEs. Here, the authors use a combinatorial peptide library to determine the chemical features that favour MGH-1 formation for short peptides and demonstrate a key role of tyrosine in this process.Joseph M. McEwenSasha FraserAlexxandra L. Sosa GuirJaydev DaveRebecca A. ScheckNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Joseph M. McEwen Sasha Fraser Alexxandra L. Sosa Guir Jaydev Dave Rebecca A. Scheck Synergistic sequence contributions bias glycation outcomes
description	Advanced glycation end-products (AGEs), such as methylglyoxal-derived hydroimidazolone isomer (MGH-1), are associated with disease and age-related disorders, and occur spontaneously, so it is unclear why specific protein sites become modified with specific AGEs. Here, the authors use a combinatorial peptide library to determine the chemical features that favour MGH-1 formation for short peptides and demonstrate a key role of tyrosine in this process.
format	article
author	Joseph M. McEwen Sasha Fraser Alexxandra L. Sosa Guir Jaydev Dave Rebecca A. Scheck
author_facet	Joseph M. McEwen Sasha Fraser Alexxandra L. Sosa Guir Jaydev Dave Rebecca A. Scheck
author_sort	Joseph M. McEwen
title	Synergistic sequence contributions bias glycation outcomes
title_short	Synergistic sequence contributions bias glycation outcomes
title_full	Synergistic sequence contributions bias glycation outcomes
title_fullStr	Synergistic sequence contributions bias glycation outcomes
title_full_unstemmed	Synergistic sequence contributions bias glycation outcomes
title_sort	synergistic sequence contributions bias glycation outcomes
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/5fba806714964ba4b997f252adebc342
work_keys_str_mv	AT josephmmcewen synergisticsequencecontributionsbiasglycationoutcomes AT sashafraser synergisticsequencecontributionsbiasglycationoutcomes AT alexxandralsosaguir synergisticsequencecontributionsbiasglycationoutcomes AT jaydevdave synergisticsequencecontributionsbiasglycationoutcomes AT rebeccaascheck synergisticsequencecontributionsbiasglycationoutcomes
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Synergistic sequence contributions bias glycation outcomes

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