Studies on the Binding Specificity of Intelectin

Our primary goal of this study was to obtain a better understanding for the carbohydrates binding interactions with human intelectin (hIntL). Studying the binding specificity of hIntL could help in discovering its natural substrate and might give us a clue about its role in the innate immune response as well as its pathophysiological action in various diseases. In this project, recombinant expression of intelectins was successfully done using HeLa cells and H5V cells. Yeast (Pachia pastoris) did not proove to be a promising expression syste m for hIntL. Using chemical synthesis, compounds (3.1–3.9) were obtained to be screened as ligands for hIntL. Herein, we used surface plasmon resonance (SPR) as our analytical tool to study hIntL binding specificity towards various synthesized Galf-containing oligosaccharides. Staudinger ligation chemistry as well as amine coupling were used to immobilize the carbohydrate epitopes to the SPR biosensor surface. Both hIntL-1 and hIntL-2 were screened against the derivatized surface.