Hydrophobic modifications at 1-phosphate of inositol 1,4,5-trisphosphate analogues enhance receptor binding.
Inositol 1,4,5-trisphosphate (IP(3)) analogues were synthesized in order to investigate the importance of the environment of 1-phosphate of IP(3) for strong binding to the IP(3) receptor. Our results show that hydrophobic modifications of the 1-phosphate moiety enhance the binding affinity, with considerable latitude of substituent structure.
Nakanishi
Waka
W
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Kikuchi
Kazuya
K
Inoue
Takanari
T
Hirose
Kenzo
K
Iino
Masamitsu
M
Nagano
Tetsuo
T
D000818:Animals; D015220:Calcium Channels / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D015544:Inositol 1,4,5-Trisphosphate / Q000031:analogs & derivatives* / Q000378:metabolism; D053496:Inositol 1,4,5-Trisphosphate Receptors; D008958:Models, Molecular; D011485:Protein Binding; D018160:Receptors, Cytoplasmic and Nuclear / Q000378:metabolism*; D013329:Structure-Activity Relationship
D015220:Calcium Channels; C506926:ITPR1 protein, human; D053496:Inositol 1,4,5-Trisphosphate Receptors; D018160:Receptors, Cytoplasmic and Nuclear; D015544:Inositol 1,4,5-Trisphosphate