An epitope is the part of a protein that is involved in protein-protein interactions. For example the part of an antigen, that is recognized by an antibody. Synthetic mimics of epitopes are rarely developed but when made they can lead to potential synthetic vaccines, interfere with undesired protein-protein interactions and ultimately can even lead to synthetic antibodies. Several factors need to be taken in to consideration when developing and evaluating epitope mimics. These include: characteristics of epitopes i.e. continuous or discontinuous, relative positioning and spatial structure. Discontinuous epitope mimics can be made by attaching the stretches of peptides that represent the epitope to a single molecular entity, for example scaffolds. The hardest part of the design remains mimicking the exact conformation of the epitope, especially for discontinuous epitopes. In this study a new improved TAC-scaffold that is suitable for sequential ligation of discontinuous epitope mimics is synthesized. By assembling three cyclic peptides on the TAC-scaffold the goal was to generate a tripodal mimic of HIV gp120. HIV infection depends on binding of the viral envelope protein gp120 to the CD4 receptor on the cell surface. During the course of this project the three peptide loops corresponding to the epitope of the HIV gp120 were successfully introduced onto the orthogonally protected trialkyne TAC-scaffold through sequential CuAAC
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