Linked Life Data

2870716

Source:http://linkedlifedata.com/resource/pubmed/id/2870716

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1986-5-14
pubmed:abstractText
The solid state molecular structures of methoxypromazine and N-monodesmethyl chlorpromazine sulphoxide were determined by X-ray crystallography, as an extension of previous studies on the molecular structures of chlorpromazine sulphoxide and methotrimeprazine sulphoxide. The binding affinities of phenothiazine drugs and metabolites with known crystal structures to dopaminergic, alpha adrenergic and muscarinic cholinergic receptors in rat brain were examined using radio-ligand binding techniques. Comparison of their solid state molecular structures and potencies in neurotransmitter receptor binding reveals that these compounds exist in two different conformations: One, associated with low biological activity, has an angle between the planes of the two aryl rings in the range of 155-160 degrees, and a torsion angle of -80 to -84 degrees around the N(10)-C bond of the side-chain, calculated from the substituted benzene ring. In the other conformation, which is found in the biologically active derivatives, the angle between the planes of the two aryl rings is in the range of 134-145 degrees, and the torsion angle around the N(10)-C bond of the side-chain is in the range of 64-69 degrees or 129-144 degrees. The "active" and "inactive" conformations thus have the side-chain on opposite sides of the ring system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1263-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Phenothiazine drugs and metabolites: molecular conformation and dopaminergic, alpha adrenergic and muscarinic cholinergic receptor binding.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't