Synthesis of dextran derivatives with thiol-specific reactive groups for the preparation of dextran-protein conjugates.
A novel strategy is described for the preparation of dextran-protein conjugates containing disulfide linkages. "Dormant" protected thiol groups are introduced as side chains on dextran. These can, in a later stage, be converted into thiol-specific reactive disulfides by reaction with (alkoxycarbonyl)sulfenyl chloride. A dextran-protein conjugate is then easily formed by reaction with a thiol group of a cysteine side chain. The disulfide linkage between dextran and the model tripeptides reduced glutathione and N-Ac-L-Cys-L-Ala-L-Lys remains intact, even after 24 h of incubation at 37 degrees C in blood.
Herman
S
S
Department of Organic Chemistry, University of Ghent, Belgium.
Persijn
G
G
Vandekerckhove
J
J
Schacht
E
E
D000595:Amino Acid Sequence; D003911:Dextrans / Q000097:blood / Q000138:chemical synthesis* / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry; D016650:Fluorescein-5-isothiocyanate; D005978:Glutathione / Q000737:chemistry; D006801:Humans; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011506:Proteins / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000097:blood / Q000737:chemistry*
D003911:Dextrans; D004220:Disulfides; D011506:Proteins; D013438:Sulfhydryl Compounds; D005978:Glutathione; D016650:Fluorescein-5-isothiocyanate