Molecular Recognition Studies on Naphthyridine Derivatives

The association constants K(b) of three hosts I–III designed to have both enhanced hydrogen bonding donor strength and conformational preorganization with biotin analogues 1–5 are reported. (1)H-NMR titrations under two different concentration conditions have been employed to determine the associati...

Descripción completa

Detalles Bibliográficos
Autores principales: Iglesias-Sánchez, José Carlos, María, Dolores Santa, Claramunt, Rosa M., Elguero, José
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6257231/
https://www.ncbi.nlm.nih.gov/pubmed/20335974
http://dx.doi.org/10.3390/molecules15031213
_version_ 1783374282423795712
author Iglesias-Sánchez, José Carlos
María, Dolores Santa
Claramunt, Rosa M.
Elguero, José
author_facet Iglesias-Sánchez, José Carlos
María, Dolores Santa
Claramunt, Rosa M.
Elguero, José
author_sort Iglesias-Sánchez, José Carlos
collection PubMed
description The association constants K(b) of three hosts I–III designed to have both enhanced hydrogen bonding donor strength and conformational preorganization with biotin analogues 1–5 are reported. (1)H-NMR titrations under two different concentration conditions have been employed to determine the association constants K(b). A statistical analysis using a presence absence matrix has been applied to calculate the different contributions. Hydrogen bond interactions make naphthyridine derivatives II and III potent binders and effective receptors for (+)-biotin methyl ester (1), due to the complex stabilization by additional hydrogen bonds.
format Online
Article
Text
id pubmed-6257231
institution National Center for Biotechnology Information
language English
publishDate 2010
publisher Molecular Diversity Preservation International
record_format MEDLINE/PubMed
spelling pubmed-62572312018-12-04 Molecular Recognition Studies on Naphthyridine Derivatives Iglesias-Sánchez, José Carlos María, Dolores Santa Claramunt, Rosa M. Elguero, José Molecules Article The association constants K(b) of three hosts I–III designed to have both enhanced hydrogen bonding donor strength and conformational preorganization with biotin analogues 1–5 are reported. (1)H-NMR titrations under two different concentration conditions have been employed to determine the association constants K(b). A statistical analysis using a presence absence matrix has been applied to calculate the different contributions. Hydrogen bond interactions make naphthyridine derivatives II and III potent binders and effective receptors for (+)-biotin methyl ester (1), due to the complex stabilization by additional hydrogen bonds. Molecular Diversity Preservation International 2010-03-03 /pmc/articles/PMC6257231/ /pubmed/20335974 http://dx.doi.org/10.3390/molecules15031213 Text en © 2010 by the authors; http://creativecommons.org/licenses/by/3.0/ licensee Molecular Diversity Preservation International, Basel, Switzerland. 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 Article
Iglesias-Sánchez, José Carlos
María, Dolores Santa
Claramunt, Rosa M.
Elguero, José
Molecular Recognition Studies on Naphthyridine Derivatives
title Molecular Recognition Studies on Naphthyridine Derivatives
title_full Molecular Recognition Studies on Naphthyridine Derivatives
title_fullStr Molecular Recognition Studies on Naphthyridine Derivatives
title_full_unstemmed Molecular Recognition Studies on Naphthyridine Derivatives
title_short Molecular Recognition Studies on Naphthyridine Derivatives
title_sort molecular recognition studies on naphthyridine derivatives
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6257231/
https://www.ncbi.nlm.nih.gov/pubmed/20335974
http://dx.doi.org/10.3390/molecules15031213
work_keys_str_mv AT iglesiassanchezjosecarlos molecularrecognitionstudiesonnaphthyridinederivatives
AT mariadoloressanta molecularrecognitionstudiesonnaphthyridinederivatives
AT claramuntrosam molecularrecognitionstudiesonnaphthyridinederivatives
AT elguerojose molecularrecognitionstudiesonnaphthyridinederivatives

Ejemplares similares