title: Stabilization of disulfide linkage in drug-polymer-immunoglobulin conjugate by microenvironmental control.
abstract: 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.
authors.affiliation: Institute of Biomedical Engineering, Tokyo Women's Medical College, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Yokoyama
authors.forename: T
authors.initials: T
authors.lastname: Okano
authors.forename: Y
authors.initials: Y
authors.lastname: Sakurai
authors.forename: K
authors.initials: K
authors.lastname: Kataoka
authors.forename: S
authors.initials: S
authors.lastname: Inoue
mesh_terms: 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
chemical_list: D004220:Disulfides; D007074:Immunoglobulin G; D011108:Polymers; D001224:Aspartic Acid; D011092:Polyethylene Glycols; D004317:Doxorubicin; D004229:Dithiothreitol