Stabilization of disulfide linkage in drug-polymer-immunoglobulin conjugate by microenvironmental control.
The stability of disulfide linkage in the conjugate composed of the anti-cancer agent adriamycin, poly(ethylene glycol)-poly(aspartic acid) block copolymer, and immunoglobulin G was studied. The disulfide linkage between the block copolymer and immunoglobulin G was found to be resistant to reduction with dithiothreitol (DTT). This extraordinary resistance is considered to be brought about by steric hindrance of the poly(aspartic acid) chain binding adriamycin.
Yokoyama
M
M
Institute of Biomedical Engineering, Tokyo Women's Medical College, Japan.
Okano
T
T
Sakurai
Y
Y
Kataoka
K
K
Inoue
S
S
D001224:Aspartic Acid; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides; D004229:Dithiothreitol; D004317:Doxorubicin; D004355:Drug Stability; D007074:Immunoglobulin G; D011092:Polyethylene Glycols / Q000138:chemical synthesis*; D011108:Polymers / Q000138:chemical synthesis*; D011485:Protein Binding; D013050:Spectrometry, Fluorescence
D004220:Disulfides; D007074:Immunoglobulin G; D011108:Polymers; D001224:Aspartic Acid; D011092:Polyethylene Glycols; D004317:Doxorubicin; D004229:Dithiothreitol