Abstract
There is a large number of proteins in nature, lectins are important since their specific interactions with glycans play key roles in variety of physiological and pathogenic processes. Lectins are not easy to be labeled, due to the weak interaction between carbohydrate and lectin. To overcome this problem, photoaffinity labeling (PAL) is a good tool to dissolve it. The photoreactive group’s function as a barb on a hook. When protein recognizes the ligand, photolysis of the probe to catch it by formation a covalent bond between probe and protein. As a result, the probe-protein complex can be purified or identified. In this thesis we synthesized the multifuntional photoaffinity probe scaffold. By the use of click reaction and amide bond formation, we can smoothly assemble galactoses and biotin tag into the probe .Furthermore, we measure the dissociation constant (Kd) between probes and proteins by Fluorescence Polarization Assay. At the same time, we evaluate its labeling yields. To compare this two data, we can prove the correlation between affinity and labeling yields.