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“Head-to-Side-Chain” Cyclodepsipeptides of Marine Origin
Since the late 1980s, a large number of depsipeptides that contain a new topography, referred to as “head-to-side-chain” cyclodepsipeptides, have been isolated and characterized. These peptides present a unique structural arrangement that comprises a macrocyclic region closed through an ester bond b...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3707169/ https://www.ncbi.nlm.nih.gov/pubmed/23697952 http://dx.doi.org/10.3390/md11051693 |
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author | Pelay-Gimeno, Marta Tulla-Puche, Judit Albericio, Fernando |
author_facet | Pelay-Gimeno, Marta Tulla-Puche, Judit Albericio, Fernando |
author_sort | Pelay-Gimeno, Marta |
collection | PubMed |
description | Since the late 1980s, a large number of depsipeptides that contain a new topography, referred to as “head-to-side-chain” cyclodepsipeptides, have been isolated and characterized. These peptides present a unique structural arrangement that comprises a macrocyclic region closed through an ester bond between the C-terminus and a β-hydroxyl group, and terminated with a polyketide moiety or a more simple branched aliphatic acid. This structural pattern, the presence of unique and complex residues, and relevant bioactivity are the main features shared by all the members of this new class of depsipeptides, which are reviewed herein. |
format | Online Article Text |
id | pubmed-3707169 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-37071692013-07-10 “Head-to-Side-Chain” Cyclodepsipeptides of Marine Origin Pelay-Gimeno, Marta Tulla-Puche, Judit Albericio, Fernando Mar Drugs Review Since the late 1980s, a large number of depsipeptides that contain a new topography, referred to as “head-to-side-chain” cyclodepsipeptides, have been isolated and characterized. These peptides present a unique structural arrangement that comprises a macrocyclic region closed through an ester bond between the C-terminus and a β-hydroxyl group, and terminated with a polyketide moiety or a more simple branched aliphatic acid. This structural pattern, the presence of unique and complex residues, and relevant bioactivity are the main features shared by all the members of this new class of depsipeptides, which are reviewed herein. MDPI 2013-05-21 /pmc/articles/PMC3707169/ /pubmed/23697952 http://dx.doi.org/10.3390/md11051693 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Pelay-Gimeno, Marta Tulla-Puche, Judit Albericio, Fernando “Head-to-Side-Chain” Cyclodepsipeptides of Marine Origin |
title | “Head-to-Side-Chain” Cyclodepsipeptides of Marine Origin |
title_full | “Head-to-Side-Chain” Cyclodepsipeptides of Marine Origin |
title_fullStr | “Head-to-Side-Chain” Cyclodepsipeptides of Marine Origin |
title_full_unstemmed | “Head-to-Side-Chain” Cyclodepsipeptides of Marine Origin |
title_short | “Head-to-Side-Chain” Cyclodepsipeptides of Marine Origin |
title_sort | “head-to-side-chain” cyclodepsipeptides of marine origin |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3707169/ https://www.ncbi.nlm.nih.gov/pubmed/23697952 http://dx.doi.org/10.3390/md11051693 |
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