Conformationally restrained carbamoylcholine homologues. Synthesis, pharmacology at neuronal nicotinic acetylcholine receptors and biostructural considerations

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Conformationally restrained carbamoylcholine homologues. Synthesis, pharmacology at neuronal nicotinic acetylcholine receptors and biostructural considerations. / de la Fuente Revenga, M; Balle, Thomas; Jensen, Anders A.; Frølund, Bente.

In: European Journal of Medicinal Chemistry, Vol. 102, 2015, p. 352-362 .

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

de la Fuente Revenga, M, Balle, T, Jensen, AA & Frølund, B 2015, 'Conformationally restrained carbamoylcholine homologues. Synthesis, pharmacology at neuronal nicotinic acetylcholine receptors and biostructural considerations', European Journal of Medicinal Chemistry, vol. 102, pp. 352-362 . https://doi.org/10.1016/j.ejmech.2015.07.029

APA

de la Fuente Revenga, M., Balle, T., Jensen, A. A., & Frølund, B. (2015). Conformationally restrained carbamoylcholine homologues. Synthesis, pharmacology at neuronal nicotinic acetylcholine receptors and biostructural considerations. European Journal of Medicinal Chemistry, 102, 352-362 . https://doi.org/10.1016/j.ejmech.2015.07.029

Vancouver

de la Fuente Revenga M, Balle T, Jensen AA, Frølund B. Conformationally restrained carbamoylcholine homologues. Synthesis, pharmacology at neuronal nicotinic acetylcholine receptors and biostructural considerations. European Journal of Medicinal Chemistry. 2015;102:352-362 . https://doi.org/10.1016/j.ejmech.2015.07.029

Author

de la Fuente Revenga, M ; Balle, Thomas ; Jensen, Anders A. ; Frølund, Bente. / Conformationally restrained carbamoylcholine homologues. Synthesis, pharmacology at neuronal nicotinic acetylcholine receptors and biostructural considerations. In: European Journal of Medicinal Chemistry. 2015 ; Vol. 102. pp. 352-362 .

Bibtex

@article{c1203c07786a4b2a99d913b71e9fea9e,
title = "Conformationally restrained carbamoylcholine homologues. Synthesis, pharmacology at neuronal nicotinic acetylcholine receptors and biostructural considerations",
abstract = "Exploration of small selective ligands for the nicotinic acetylcholine receptors (nAChRs) based on acetylcholine (ACh) has led to the development of potent agonists with clear preference for the α4β2 nAChR, the most prevalent nAChR subtype in the central nervous system. In this work we present the continuation of these efforts aimed at increasing this subtype selectivity by introduction of conformational restriction in the carbamoylcholine homologue, 3-(dimethylaminobutyl) dimethylcarbamate (DMABC). Our results highlight the importance of the N-carbamoyl substitution in α4β2-subtype selectivity. Moreover, we have confirmed the non-linear conformation of DMABC bound to nAChRs suggested by recent crystal structures of the compound in complex with the Lymnaea stagnalis ACh binding protein.",
author = "{de la Fuente Revenga}, M and Thomas Balle and Jensen, {Anders A.} and Bente Fr{\o}lund",
year = "2015",
doi = "10.1016/j.ejmech.2015.07.029",
language = "English",
volume = "102",
pages = "352--362 ",
journal = "European Journal of Medicinal Chemistry",
issn = "0223-5234",
publisher = "Elsevier Masson",

}

RIS

TY - JOUR

T1 - Conformationally restrained carbamoylcholine homologues. Synthesis, pharmacology at neuronal nicotinic acetylcholine receptors and biostructural considerations

AU - de la Fuente Revenga, M

AU - Balle, Thomas

AU - Jensen, Anders A.

AU - Frølund, Bente

PY - 2015

Y1 - 2015

N2 - Exploration of small selective ligands for the nicotinic acetylcholine receptors (nAChRs) based on acetylcholine (ACh) has led to the development of potent agonists with clear preference for the α4β2 nAChR, the most prevalent nAChR subtype in the central nervous system. In this work we present the continuation of these efforts aimed at increasing this subtype selectivity by introduction of conformational restriction in the carbamoylcholine homologue, 3-(dimethylaminobutyl) dimethylcarbamate (DMABC). Our results highlight the importance of the N-carbamoyl substitution in α4β2-subtype selectivity. Moreover, we have confirmed the non-linear conformation of DMABC bound to nAChRs suggested by recent crystal structures of the compound in complex with the Lymnaea stagnalis ACh binding protein.

AB - Exploration of small selective ligands for the nicotinic acetylcholine receptors (nAChRs) based on acetylcholine (ACh) has led to the development of potent agonists with clear preference for the α4β2 nAChR, the most prevalent nAChR subtype in the central nervous system. In this work we present the continuation of these efforts aimed at increasing this subtype selectivity by introduction of conformational restriction in the carbamoylcholine homologue, 3-(dimethylaminobutyl) dimethylcarbamate (DMABC). Our results highlight the importance of the N-carbamoyl substitution in α4β2-subtype selectivity. Moreover, we have confirmed the non-linear conformation of DMABC bound to nAChRs suggested by recent crystal structures of the compound in complex with the Lymnaea stagnalis ACh binding protein.

U2 - 10.1016/j.ejmech.2015.07.029

DO - 10.1016/j.ejmech.2015.07.029

M3 - Journal article

C2 - 26298493

VL - 102

SP - 352

EP - 362

JO - European Journal of Medicinal Chemistry

JF - European Journal of Medicinal Chemistry

SN - 0223-5234

ER -

ID: 141260854