TY - JOUR
T1 - Concise synthesis of ciguatoxin ABC-ring fragments and surface plasmon resonance study of the interaction of their BSA conjugates with monoclonal antibodies
AU - Nagumo, Yoko
AU - Oguri, Hiroki
AU - Shindo, Yumi
AU - Sasaki, Shin ya
AU - Oishi, Tohru
AU - Hirama, Masahiro
AU - Tomioka, Yoshihisa
AU - Mizugaki, Michinao
AU - Tsumuraya, Takeshi
N1 - Funding Information:
The authors are grateful to Dr. Keiichi Konoki (The University of Tokyo), Dr. Goh Matsuo (RIKEN), Mr. Kazunobu Asano (BIACORE), and Dr. Junichi Inagawa (BIACORE) for their helpful comments. A fellowship to Y.N. from the Japanese Society for the Promotion of Science is gratefully acknowledged.
PY - 2001/8/6
Y1 - 2001/8/6
N2 - Monoclonal antibodies (mAbs), 4H2 and 6H7, were prepared previously using a protein conjugate of a 1:1 epimeric mixture of the synthetic ABC-ring fragments of ciguatoxin (CTX), 3 and 4. Here, the interactions of these mAbs with the fragments of CTX and CTX3C, 3 and 5, were investigated by surface plasmon resonance (SPR) spectroscopy in an attempt to clarify an antigenic determinant. Compared with the previous synthesis, the fragment 3 possessing the 2S configuration was synthesized from tri-O-acetyl-D-glucal much more effectively. The mAb 4H2 was already known to show a dose-dependent binding to the bovine serum albumin (BSA) conjugate of 3, but not to that of 5. The present SPR study of 4H2 demonstrates that the A-ring side chain of 3 plays a decisive role as an epitope. Therefore, SPR can effectively replace the ELISA method for the analysis of mAbs.
AB - Monoclonal antibodies (mAbs), 4H2 and 6H7, were prepared previously using a protein conjugate of a 1:1 epimeric mixture of the synthetic ABC-ring fragments of ciguatoxin (CTX), 3 and 4. Here, the interactions of these mAbs with the fragments of CTX and CTX3C, 3 and 5, were investigated by surface plasmon resonance (SPR) spectroscopy in an attempt to clarify an antigenic determinant. Compared with the previous synthesis, the fragment 3 possessing the 2S configuration was synthesized from tri-O-acetyl-D-glucal much more effectively. The mAb 4H2 was already known to show a dose-dependent binding to the bovine serum albumin (BSA) conjugate of 3, but not to that of 5. The present SPR study of 4H2 demonstrates that the A-ring side chain of 3 plays a decisive role as an epitope. Therefore, SPR can effectively replace the ELISA method for the analysis of mAbs.
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U2 - 10.1016/S0960-894X(01)00358-4
DO - 10.1016/S0960-894X(01)00358-4
M3 - Article
C2 - 11454475
AN - SCOPUS:0035817276
SN - 0960-894X
VL - 11
SP - 2037
EP - 2040
JO - Bioorganic and Medicinal Chemistry Letters
JF - Bioorganic and Medicinal Chemistry Letters
IS - 15
ER -