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Reversible Covalent End‐Capping of Collagen Model Peptides
The combination of supramolecular aggregation of collagen model peptides with reversible covalent end‐capping of the formed triple helix in a single experimental set‐up yielded minicollagens, which were characterized by a single melting temperature. In spite of the numerous possible reaction interme...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6900188/ https://www.ncbi.nlm.nih.gov/pubmed/31557356 http://dx.doi.org/10.1002/chem.201903460 |
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author | Priem, Christoph Geyer, Armin |
author_facet | Priem, Christoph Geyer, Armin |
author_sort | Priem, Christoph |
collection | PubMed |
description | The combination of supramolecular aggregation of collagen model peptides with reversible covalent end‐capping of the formed triple helix in a single experimental set‐up yielded minicollagens, which were characterized by a single melting temperature. In spite of the numerous possible reaction intermediates, a specific synthetic collagen with a leading, middle and trailing strand is formed in a highly cooperative self‐assembly process. |
format | Online Article Text |
id | pubmed-6900188 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-69001882019-12-20 Reversible Covalent End‐Capping of Collagen Model Peptides Priem, Christoph Geyer, Armin Chemistry Communications The combination of supramolecular aggregation of collagen model peptides with reversible covalent end‐capping of the formed triple helix in a single experimental set‐up yielded minicollagens, which were characterized by a single melting temperature. In spite of the numerous possible reaction intermediates, a specific synthetic collagen with a leading, middle and trailing strand is formed in a highly cooperative self‐assembly process. John Wiley and Sons Inc. 2019-10-17 2019-11-13 /pmc/articles/PMC6900188/ /pubmed/31557356 http://dx.doi.org/10.1002/chem.201903460 Text en © 2019 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Communications Priem, Christoph Geyer, Armin Reversible Covalent End‐Capping of Collagen Model Peptides |
title | Reversible Covalent End‐Capping of Collagen Model Peptides |
title_full | Reversible Covalent End‐Capping of Collagen Model Peptides |
title_fullStr | Reversible Covalent End‐Capping of Collagen Model Peptides |
title_full_unstemmed | Reversible Covalent End‐Capping of Collagen Model Peptides |
title_short | Reversible Covalent End‐Capping of Collagen Model Peptides |
title_sort | reversible covalent end‐capping of collagen model peptides |
topic | Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6900188/ https://www.ncbi.nlm.nih.gov/pubmed/31557356 http://dx.doi.org/10.1002/chem.201903460 |
work_keys_str_mv | AT priemchristoph reversiblecovalentendcappingofcollagenmodelpeptides AT geyerarmin reversiblecovalentendcappingofcollagenmodelpeptides |