Biochemical analysis of cellular target of S-trityl-L-cysteine derivatives using affinity matrix.
Biochemical analysis of the cellular target of S-trityl-l-cysteine (STLC) derivatives was performed by using the newly synthesized STLC derivative-immobilized affinity beads (3d). The affinity beads efficiently captured KSP in HCT116 cytoplasmic cell lysate. The results obtained from pull-down and competition experiments using 3d with STLC derivatives provided the first evidence for direct interaction of these derivatives with KSP in cancer cells. Design, synthesis and application of 3d were reported.
Shimizu
Makiko
M
Center for Drug Discovery, Graduate School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan.
Ishii
Hirosuke
H
Ogo
Naohisa
N
Matsuno
Kenji
K
Asai
Akira
A
D000970:Antineoplastic Agents / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D045744:Cell Line, Tumor; D003545:Cysteine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D006801:Humans; D055767:Immobilized Proteins / Q000737:chemistry / Q000378:metabolism; D016547:Kinesins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011485:Protein Binding
D000970:Antineoplastic Agents; D004791:Enzyme Inhibitors; D055767:Immobilized Proteins; C470243:KIF11 protein, human; C003724:3-tritylthio-L-alanine; D016547:Kinesins; D003545:Cysteine