Abstract
Proteins are important for preserving life. Their highly complex surface imparts functionalities that are
only found in proteins. Through specific sites on their surface they can interact with one another to carry
out several biological functions, such as DNA replication, signal transduction, immune response and
apoptosis. However, infectious proteins can also interact with physiological proteins inside a living
organism. This results in harming the organism which can even lead to death. Nevertheless, by
administrating a molecule that generates therapeutic antibodies can save the day. The problem is the
easiest way that can be done is by using a natural protein, however, proteins are known as bad drugs
candidates, basically due to degradation that exhibit inside the body. A novel solution would be to recreate the “hot spots” of a protein in a considerable smaller molecule, i.e. to mimic the protein.
A good way to do that is to connect linear peptides, which bear the antigenic sites of a protein, on an
organic molecule (scaffold). This molecular scaffold has to induce certain conformation on the peptides
and stability. Moreover, reactions that are applicable to unprotected peptides (“Click Chemistry”) are
needed so that protective groups are absent in the synthesis.