N-SUBSTITUTION AND á1-ADRENERGIC RECEPTOR AFFINITY OF LAUDANOSINE ANALOGUES

Benzyltetrahydroisoquinoline (BTHIQ) molecules are able to adopt widely differing conformations that depend on the presence or absence of N-substituents. To assess the possible role of BTHIQ conformation on the affinity of these compounds for a 1-adrenergic receptors, of interest for the management...

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Autores principales:	ITURRIAGA-VÁSQUEZ,PATRICIO, CASSELS,BRUCE K, IVORRA,M. DOLORES, D'OCON,M. PILAR
Lenguaje:	English
Publicado:	Sociedad Chilena de Química 2006
Materias:	a 1-adrenergic receptor binding norlaudanosine laudanosine N-alkylnorlaudanosines benzyltetrahydroisoquinolines tetrahydropalmatine glaucine
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-97072006000300001
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spelling	oai:scielo:S0717-970720060003000012006-11-16N-SUBSTITUTION AND á1-ADRENERGIC RECEPTOR AFFINITY OF LAUDANOSINE ANALOGUESITURRIAGA-VÁSQUEZ,PATRICIOCASSELS,BRUCE KIVORRA,M. DOLORESD'OCON,M. PILAR a 1-adrenergic receptor binding norlaudanosine laudanosine N-alkylnorlaudanosines benzyltetrahydroisoquinolines tetrahydropalmatine glaucine Benzyltetrahydroisoquinoline (BTHIQ) molecules are able to adopt widely differing conformations that depend on the presence or absence of N-substituents. To assess the possible role of BTHIQ conformation on the affinity of these compounds for a 1-adrenergic receptors, of interest for the management of hypertension, the racemic N-unsubstituted BTHIQ norlaudanosine and a series of N-alkylated derivatives were assessed for binding to rat brain cortical sites labelled with the radioligand [³H]prazosin. The a 1-adrenergic affinity in this series increased with the bulk of the substituent on the nitrogen atom, from the N-ethyl to the N-propyl analogue. Comparison of these results with published data for related BTHIQs and for the rigid mimics of the fully extended and semi-folded conformations of laudanosine, tetrahydropalmatine and glaucine, suggested that the a 1-adrenergic receptor binding site is able to accommodate either conformation. The presence of a bulky substituent on the nitrogen atom seems to favor receptor binding independently of the favored conformation, and that the orientation in which BTHIQs are bound probably differs depending on the presence or absence of a hydroxyl group at a key positioninfo:eu-repo/semantics/openAccessSociedad Chilena de QuímicaJournal of the Chilean Chemical Society v.51 n.3 20062006-09-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-97072006000300001en10.4067/S0717-97072006000300001
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	a 1-adrenergic receptor binding norlaudanosine laudanosine N-alkylnorlaudanosines benzyltetrahydroisoquinolines tetrahydropalmatine glaucine
spellingShingle	a 1-adrenergic receptor binding norlaudanosine laudanosine N-alkylnorlaudanosines benzyltetrahydroisoquinolines tetrahydropalmatine glaucine ITURRIAGA-VÁSQUEZ,PATRICIO CASSELS,BRUCE K IVORRA,M. DOLORES D'OCON,M. PILAR N-SUBSTITUTION AND á1-ADRENERGIC RECEPTOR AFFINITY OF LAUDANOSINE ANALOGUES
description	Benzyltetrahydroisoquinoline (BTHIQ) molecules are able to adopt widely differing conformations that depend on the presence or absence of N-substituents. To assess the possible role of BTHIQ conformation on the affinity of these compounds for a 1-adrenergic receptors, of interest for the management of hypertension, the racemic N-unsubstituted BTHIQ norlaudanosine and a series of N-alkylated derivatives were assessed for binding to rat brain cortical sites labelled with the radioligand [³H]prazosin. The a 1-adrenergic affinity in this series increased with the bulk of the substituent on the nitrogen atom, from the N-ethyl to the N-propyl analogue. Comparison of these results with published data for related BTHIQs and for the rigid mimics of the fully extended and semi-folded conformations of laudanosine, tetrahydropalmatine and glaucine, suggested that the a 1-adrenergic receptor binding site is able to accommodate either conformation. The presence of a bulky substituent on the nitrogen atom seems to favor receptor binding independently of the favored conformation, and that the orientation in which BTHIQs are bound probably differs depending on the presence or absence of a hydroxyl group at a key position
author	ITURRIAGA-VÁSQUEZ,PATRICIO CASSELS,BRUCE K IVORRA,M. DOLORES D'OCON,M. PILAR
author_facet	ITURRIAGA-VÁSQUEZ,PATRICIO CASSELS,BRUCE K IVORRA,M. DOLORES D'OCON,M. PILAR
author_sort	ITURRIAGA-VÁSQUEZ,PATRICIO
title	N-SUBSTITUTION AND á1-ADRENERGIC RECEPTOR AFFINITY OF LAUDANOSINE ANALOGUES
title_short	N-SUBSTITUTION AND á1-ADRENERGIC RECEPTOR AFFINITY OF LAUDANOSINE ANALOGUES
title_full	N-SUBSTITUTION AND á1-ADRENERGIC RECEPTOR AFFINITY OF LAUDANOSINE ANALOGUES
title_fullStr	N-SUBSTITUTION AND á1-ADRENERGIC RECEPTOR AFFINITY OF LAUDANOSINE ANALOGUES
title_full_unstemmed	N-SUBSTITUTION AND á1-ADRENERGIC RECEPTOR AFFINITY OF LAUDANOSINE ANALOGUES
title_sort	n-substitution and á1-adrenergic receptor affinity of laudanosine analogues
publisher	Sociedad Chilena de Química
publishDate	2006
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-97072006000300001
work_keys_str_mv	AT iturriagavasquezpatricio nsubstitutionanda1adrenergicreceptoraffinityoflaudanosineanalogues AT casselsbrucek nsubstitutionanda1adrenergicreceptoraffinityoflaudanosineanalogues AT ivorramdolores nsubstitutionanda1adrenergicreceptoraffinityoflaudanosineanalogues AT doconmpilar nsubstitutionanda1adrenergicreceptoraffinityoflaudanosineanalogues
_version_	1718445362474123264

N-SUBSTITUTION AND á1-ADRENERGIC RECEPTOR AFFINITY OF LAUDANOSINE ANALOGUES

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