Conformational studies on resiniferatoxin (RTX), an ultrapotent vanilloid agonist

Sam F. Victory; Giovanni Appendino; David G.Vander Velde

doi:10.1016/S0968-0896(97)10029-3

Conformational studies on resiniferatoxin (RTX), an ultrapotent vanilloid agonist

Sam F. Victory, Giovanni Appendino, David G.Vander Velde

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

Abstract

In polar solution, NOE studies show a pronounced clustering of the aromatic moieties (9,13,14-phenylacetate orthoester and 20-homovanillate) of the ultrapotent vanilloid agonist resiniferatoxin (RTX). This clustering is absent in nonpolar solution. Low energy clustered structures from molecular dynamics simulations account for the observed NOEs. These results suggest that the phenylorthoacetate moiety can assist the attainment of specific alignments between the terpenoid core and the vanillyl moiety, possibly preorganizing them for ideal receptor binding.

Lingua originale	Inglese
pagine (da-a)	223-229
Numero di pagine	7
Rivista	Bioorganic and Medicinal Chemistry
Volume	6
Numero di pubblicazione	2
DOI	https://doi.org/10.1016/S0968-0896(97)10029-3
Stato di pubblicazione	Pubblicato - 1 feb 1998
Pubblicato esternamente	Sì

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10.1016/S0968-0896(97)10029-3

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title = "Conformational studies on resiniferatoxin (RTX), an ultrapotent vanilloid agonist",

abstract = "In polar solution, NOE studies show a pronounced clustering of the aromatic moieties (9,13,14-phenylacetate orthoester and 20-homovanillate) of the ultrapotent vanilloid agonist resiniferatoxin (RTX). This clustering is absent in nonpolar solution. Low energy clustered structures from molecular dynamics simulations account for the observed NOEs. These results suggest that the phenylorthoacetate moiety can assist the attainment of specific alignments between the terpenoid core and the vanillyl moiety, possibly preorganizing them for ideal receptor binding.",

keywords = "Conformation, Hydrophobic collapse, NMR, Resiniferatoxin",

author = "Victory, \{Sam F.\} and Giovanni Appendino and Velde, \{David G.Vander\}",

note = "Funding Information: The authors thank the Kansas Health Foundation for a postdoctoral fellowship awarded to SFV; and Arpad Szallasi, Department of Anatomy and Neurobiology, Washington University School of Medicine, St Louis, MO, Peter Blumberg, National Cancer Institute, Bethesda, MD, and Cynthia Larive, University of Kansas, for helpful discussions. ",

year = "1998",

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doi = "10.1016/S0968-0896(97)10029-3",

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AU - Victory, Sam F.

AU - Appendino, Giovanni

AU - Velde, David G.Vander

N1 - Funding Information: The authors thank the Kansas Health Foundation for a postdoctoral fellowship awarded to SFV; and Arpad Szallasi, Department of Anatomy and Neurobiology, Washington University School of Medicine, St Louis, MO, Peter Blumberg, National Cancer Institute, Bethesda, MD, and Cynthia Larive, University of Kansas, for helpful discussions.

PY - 1998/2/1

Y1 - 1998/2/1

N2 - In polar solution, NOE studies show a pronounced clustering of the aromatic moieties (9,13,14-phenylacetate orthoester and 20-homovanillate) of the ultrapotent vanilloid agonist resiniferatoxin (RTX). This clustering is absent in nonpolar solution. Low energy clustered structures from molecular dynamics simulations account for the observed NOEs. These results suggest that the phenylorthoacetate moiety can assist the attainment of specific alignments between the terpenoid core and the vanillyl moiety, possibly preorganizing them for ideal receptor binding.

AB - In polar solution, NOE studies show a pronounced clustering of the aromatic moieties (9,13,14-phenylacetate orthoester and 20-homovanillate) of the ultrapotent vanilloid agonist resiniferatoxin (RTX). This clustering is absent in nonpolar solution. Low energy clustered structures from molecular dynamics simulations account for the observed NOEs. These results suggest that the phenylorthoacetate moiety can assist the attainment of specific alignments between the terpenoid core and the vanillyl moiety, possibly preorganizing them for ideal receptor binding.

KW - Conformation

KW - Hydrophobic collapse

KW - NMR

KW - Resiniferatoxin

UR - https://www.scopus.com/pages/publications/0031810017

U2 - 10.1016/S0968-0896(97)10029-3

DO - 10.1016/S0968-0896(97)10029-3

M3 - Article

SN - 0968-0896

VL - 6

SP - 223

EP - 229

JO - Bioorganic and Medicinal Chemistry

JF - Bioorganic and Medicinal Chemistry

IS - 2

ER -

Conformational studies on resiniferatoxin (RTX), an ultrapotent vanilloid agonist

Abstract

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