A Structure-Activity Study of Antibacterial Diterpenoids

An analysis of the antibacterial activities of 15 terpenoids, eleven of which were previously described by us and four were extracted from the literature, suggested two structural requirements for activity of these and related compounds: a hydrophobic moiety, consisting of a substituted decalin skel...

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Autores principales: Urzúa, Alejandro, Rezende,  Marcos C., Mascayano, Carolina, Vásquez, Loretta
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2008
Materias:
Full Paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6245368/
https://www.ncbi.nlm.nih.gov/pubmed/18463590
http://dx.doi.org/10.3390/molecules13040822
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author Urzúa, Alejandro
Rezende,  Marcos C.
Mascayano, Carolina
Vásquez, Loretta
author_facet Urzúa, Alejandro
Rezende,  Marcos C.
Mascayano, Carolina
Vásquez, Loretta
author_sort Urzúa, Alejandro
collection PubMed
description An analysis of the antibacterial activities of 15 terpenoids, eleven of which were previously described by us and four were extracted from the literature, suggested two structural requirements for activity of these and related compounds: a hydrophobic moiety, consisting of a substituted decalin skeleton, and a hydrophilic region possessing one hydrogen-bond-donor group. These structural requirements are responsible for an optimal insertion of these and related compounds into cell membranes, as suggested by the results of docking some of these compounds into a model phospholipid bilayer.
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spelling pubmed-62453682018-11-26 A Structure-Activity Study of Antibacterial Diterpenoids Urzúa, Alejandro Rezende,  Marcos C. Mascayano, Carolina Vásquez, Loretta Molecules Full Paper An analysis of the antibacterial activities of 15 terpenoids, eleven of which were previously described by us and four were extracted from the literature, suggested two structural requirements for activity of these and related compounds: a hydrophobic moiety, consisting of a substituted decalin skeleton, and a hydrophilic region possessing one hydrogen-bond-donor group. These structural requirements are responsible for an optimal insertion of these and related compounds into cell membranes, as suggested by the results of docking some of these compounds into a model phospholipid bilayer. MDPI 2008-04-17 /pmc/articles/PMC6245368/ /pubmed/18463590 http://dx.doi.org/10.3390/molecules13040822 Text en © 2008 by MDPI (http://www.mdpi.org). Reproduction is permitted for noncommercial purposes.
spellingShingle Full Paper
Urzúa, Alejandro
Rezende,  Marcos C.
Mascayano, Carolina
Vásquez, Loretta
A Structure-Activity Study of Antibacterial Diterpenoids
title A Structure-Activity Study of Antibacterial Diterpenoids
title_full A Structure-Activity Study of Antibacterial Diterpenoids
title_fullStr A Structure-Activity Study of Antibacterial Diterpenoids
title_full_unstemmed A Structure-Activity Study of Antibacterial Diterpenoids
title_short A Structure-Activity Study of Antibacterial Diterpenoids
title_sort structure-activity study of antibacterial diterpenoids
topic Full Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6245368/
https://www.ncbi.nlm.nih.gov/pubmed/18463590
http://dx.doi.org/10.3390/molecules13040822
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