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Diversity-oriented synthesis of analogues of the novel macrocyclic peptide FR-225497 through late stage functionalization

A concise synthetic approach to a class of biologically interesting cyclic tetrapeptides is reported which involves a late-stage functionalization of a macrocyclic scaffold through cross metathesis in an attempt to create diversity. The utility of this protocol is demonstrated through the preparatio...

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Detalles Bibliográficos
Autores principales: Mukherjee, Jyotiprasad, Sil, Suman, Chattopadhyay, Shital Kumar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Beilstein-Institut 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4685926/
https://www.ncbi.nlm.nih.gov/pubmed/26734096
http://dx.doi.org/10.3762/bjoc.11.270
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author Mukherjee, Jyotiprasad
Sil, Suman
Chattopadhyay, Shital Kumar
author_facet Mukherjee, Jyotiprasad
Sil, Suman
Chattopadhyay, Shital Kumar
author_sort Mukherjee, Jyotiprasad
collection PubMed
description A concise synthetic approach to a class of biologically interesting cyclic tetrapeptides is reported which involves a late-stage functionalization of a macrocyclic scaffold through cross metathesis in an attempt to create diversity. The utility of this protocol is demonstrated through the preparation of three structural analogues of the important naturally occurring histone deacetylase inhibitor FR-225497.
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spelling pubmed-46859262016-01-05 Diversity-oriented synthesis of analogues of the novel macrocyclic peptide FR-225497 through late stage functionalization Mukherjee, Jyotiprasad Sil, Suman Chattopadhyay, Shital Kumar Beilstein J Org Chem Full Research Paper A concise synthetic approach to a class of biologically interesting cyclic tetrapeptides is reported which involves a late-stage functionalization of a macrocyclic scaffold through cross metathesis in an attempt to create diversity. The utility of this protocol is demonstrated through the preparation of three structural analogues of the important naturally occurring histone deacetylase inhibitor FR-225497. Beilstein-Institut 2015-12-08 /pmc/articles/PMC4685926/ /pubmed/26734096 http://dx.doi.org/10.3762/bjoc.11.270 Text en Copyright © 2015, Mukherjee et al. https://creativecommons.org/licenses/by/2.0https://www.beilstein-journals.org/bjoc/termsThis is an Open Access article under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The license is subject to the Beilstein Journal of Organic Chemistry terms and conditions: (https://www.beilstein-journals.org/bjoc/terms)
spellingShingle Full Research Paper
Mukherjee, Jyotiprasad
Sil, Suman
Chattopadhyay, Shital Kumar
Diversity-oriented synthesis of analogues of the novel macrocyclic peptide FR-225497 through late stage functionalization
title Diversity-oriented synthesis of analogues of the novel macrocyclic peptide FR-225497 through late stage functionalization
title_full Diversity-oriented synthesis of analogues of the novel macrocyclic peptide FR-225497 through late stage functionalization
title_fullStr Diversity-oriented synthesis of analogues of the novel macrocyclic peptide FR-225497 through late stage functionalization
title_full_unstemmed Diversity-oriented synthesis of analogues of the novel macrocyclic peptide FR-225497 through late stage functionalization
title_short Diversity-oriented synthesis of analogues of the novel macrocyclic peptide FR-225497 through late stage functionalization
title_sort diversity-oriented synthesis of analogues of the novel macrocyclic peptide fr-225497 through late stage functionalization
topic Full Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4685926/
https://www.ncbi.nlm.nih.gov/pubmed/26734096
http://dx.doi.org/10.3762/bjoc.11.270
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