Binding of tryptamine analogs at h5-HT1E receptors: a structure-affinity investigation.
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.
Dukat
Małgorzata
M
Department of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23298, USA.
Smith
Carol
C
Herrick-Davis
Katharine
K
Teitler
Milt
M
Glennon
Richard A
RA
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*
D011985:Receptors, Serotonin; D014363:Tryptamines; C076396:serotonin 1E receptor; D012701:Serotonin; C030820:tryptamine