title: Binding of tryptamine analogs at h5-HT1E receptors: a structure-affinity investigation.
abstract: Structure-affinity requirements for the binding of serotonin (5-HT) analogs at human 5-HT1E receptors were investigated by examining the affinities of >40 tryptamine-related compounds. No tryptamine analog was found to bind with substantially higher affinity than 5-HT. The results indicate that hydrogen bonding plays a key role in the 5-HT1E/receptor interaction. This finding was supported using quantitative structure-activity analysis (QSAR) techniques such as comparative molecular field analysis (CoMFA) and the program QsarIS.
authors.affiliation: Department of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23298, USA.
authors.forename: Małgorzata
authors.initials: M
authors.lastname: Dukat
authors.forename: Carol
authors.initials: C
authors.lastname: Smith
authors.forename: Katharine
authors.initials: K
authors.lastname: Herrick-Davis
authors.forename: Milt
authors.initials: M
authors.lastname: Teitler
authors.forename: Richard A
authors.initials: RA
authors.lastname: Glennon
mesh_terms: D002460:Cell Line; D006801:Humans; D008968:Molecular Conformation; D015394:Molecular Structure; D021281:Quantitative Structure-Activity Relationship; D011869:Radioligand Assay; D011985:Receptors, Serotonin / Q000378:metabolism*; D012701:Serotonin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D014363:Tryptamines / Q000737:chemistry*
chemical_list: D011985:Receptors, Serotonin; D014363:Tryptamines; C076396:serotonin 1E receptor; D012701:Serotonin; C030820:tryptamine