lewis-y-antigen and maleimide

lewis-y-antigen has been researched along with maleimide* in 1 studies

Other Studies

1 other study(ies) available for lewis-y-antigen and maleimide

Article	Year
The immunogenicity of the tumor-associated antigen Lewis(y) may be suppressed by a bifunctional cross-linker required for coupling to a carrier protein. Chemistry (Weinheim an der Bergstrasse, Germany), 2004, Jul-19, Volume: 10, Issue:14 A Lewis(y) (Le(y)) tetrasaccharide modified by an artificial aminopropyl spacer was synthesized by a highly convergent approach that employed a levulinoyl ester and a 9-fluorenylmethoxycarbonate for temporary protection of the hydroxy groups and a trichloroethyloxycarbonyl as an amino protecting group. The artificial aminopropyl moiety was modified by a thioacetyl group, which allowed efficient conjugation to keyhole limpet hemocyanin (KLH) modified by electrophilic 4-(maleimidomethyl)cyclohexane-1-carboxylate (MI). Mice were immunized with the KLH-MI-Le(y) antigen. A detailed analysis of sera by ELISA established that a strong immunoglobulin G (IgG) antibody response was elicited against the linker region. The use of a smaller and more flexible 3-(bromoacetamido)propionate for the attachment of Le(y) to KLH not only reduced the IgG antibody response against the linker but also led to a significantly improved immune response against the Le(y) antigen. This study shows that highly antigenic linkers suppress antibody responses to weak antigens such as self-antigens. Topics: Antibodies; Carbohydrate Conformation; Carrier Proteins; Cross-Linking Reagents; Enzyme-Linked Immunosorbent Assay; Hydrolysis; Immunization; Immunogenetics; Lewis Blood Group Antigens; Maleimides; Neoplasms; Polysaccharides; Protein Binding	2004

Article

Year

The immunogenicity of the tumor-associated antigen Lewis(y) may be suppressed by a bifunctional cross-linker required for coupling to a carrier protein.

Chemistry (Weinheim an der Bergstrasse, Germany), 2004, Jul-19, Volume: 10, Issue:14

A Lewis(y) (Le(y)) tetrasaccharide modified by an artificial aminopropyl spacer was synthesized by a highly convergent approach that employed a levulinoyl ester and a 9-fluorenylmethoxycarbonate for temporary protection of the hydroxy groups and a trichloroethyloxycarbonyl as an amino protecting group. The artificial aminopropyl moiety was modified by a thioacetyl group, which allowed efficient conjugation to keyhole limpet hemocyanin (KLH) modified by electrophilic 4-(maleimidomethyl)cyclohexane-1-carboxylate (MI). Mice were immunized with the KLH-MI-Le(y) antigen. A detailed analysis of sera by ELISA established that a strong immunoglobulin G (IgG) antibody response was elicited against the linker region. The use of a smaller and more flexible 3-(bromoacetamido)propionate for the attachment of Le(y) to KLH not only reduced the IgG antibody response against the linker but also led to a significantly improved immune response against the Le(y) antigen. This study shows that highly antigenic linkers suppress antibody responses to weak antigens such as self-antigens.

Topics: Antibodies; Carbohydrate Conformation; Carrier Proteins; Cross-Linking Reagents; Enzyme-Linked Immunosorbent Assay; Hydrolysis; Immunization; Immunogenetics; Lewis Blood Group Antigens; Maleimides; Neoplasms; Polysaccharides; Protein Binding

2004