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Relevant academic research and scientific papers

Development of Clickable Monophosphoryl Lipid A Derivatives toward Semisynthetic Conjugates with Tumor-Associated Carbohydrate Antigens

A semisynthetic strategy to obtain monophosphoryl lipid A derivatives equipped with clickable (azide, alkyne, double bond, or thiol precursor) moieties, starting from the native lipid A isolated from Escherichia coli, is presented. These lipid A derivatives can be conjugated with other interesting biomolecules, such as tumor-associated carbohydrate antigens (TACAs). In this way, the immunostimulant activity of monophosphoryl lipid A can significantly improve the immunogenicity of TACAs, thus opening access to potential self-adjuvant anticancer vaccine candidates. A monophosphoryl lipid A-Thomson-Friedenreich (TF) antigen conjugate was obtained to demonstrate the feasibility of this methodology, which stands as a valuable, rapid, and scalable alternative to the highly complex approaches of total synthesis recently reported to the same aim. A preliminary evaluation of the immunological activity of this conjugate as well as of other semisynthetic lipid A derivatives was also reported.

Simultaneous binding of mouse monoclonal antibody and streptavidin to heterobifunctional dendritic L-lysine core bearing T-antigen tumor marker and biotin

Thiolate T-antigen Galβ-(1-3)-GalNAcα, T-Ag] (6 ), derive in situ from thioacetate 5 was couple to N-chloroacetylate glycylglycyl L-lysine dendritic cores (7 9) using high yielding substitution reactions to affor di- (10), tetra- (11), and octa-valent (12) glycodendrimers in good yields (76 86%). Heterobifunctional conjugate 14 was prepare as a biosensor from tetravalent conjugate 11 an biotin hydrazide 13 using TBTU strategy. In a solid-phase double sandwich enzyme linked immuno-sorbent assays (ELISA), biotinylate conjugate 14 was shown to bin to streptavidin used as a coating material. Mouse monoclonal anti T-Ag antibody (IgG3) an horseradish peroxydase-labele goat anti mouse IgG, used for quantification, were found to bind T-Ag tetramer 14 immobilize on the surface of the streptavin layer. A typical saturation curve was observed for 14 while non-biotinylated tetramer 11 showed no binding in the entire concentration range. These results demonstrate the availability of both haptens toward the T-Ag antibody and streptavidin receptors. Copyright

Synthesis and Evaluation of Glycoconjugates Comprising N-Acyl-Modified Thomsen-Friedenreich Antigens as Anticancer Vaccines

Thomsen-Friedenreich (TF) antigen is an important tumor-associated carbohydrate antigen. Its low immunogenicity, however, limits its application in the development of anticancer vaccines. To solve this problem, several N-acyl-modified TF derivatives were synthesized and conjugated with carrier protein CRM197 (a mutated diphtheria toxoid cross-reactive material). The immunological results in BALB/c mice demonstrated that these modified TF antigen conjugates could stimulate the production of higher titers of IgG antibodies that cross-reacted with native TF antigen. These glycoconjugates showed strong lymphocyte proliferative response, suggesting that they can induce cellular immunity. Furthermore, the elicited antisera reacted strongly with TF-positive tumor cells (4T1). In particular, the N-monofluoroacetyl-modified TF conjugate 4-CRM197 showed the strongest complement-dependent cytotoxicity effect against 4T1 cells, implying the potential of this glycoconjugate as an anticancer vaccine. Recruiting the IgG army: Several N-modified TF antigen derivatives were synthesized and conjugated with the carrier protein CRM197. These glycoconjugates significantly increased the titers of antibodies than can recognize the native TF antigen and kill tumor cells, thus having the potential for use as carbohydrate-based anticancer vaccines.