The protein mimetics

Course Description

Despite their enormous diversity in biological function and structure, the use of peptides and proteins as drugs is limited due to their low metabolic stability, poor absorption after oral administration, rapid excretion and undesired effects caused by interaction of the conformationally flexible peptides and proteins with various receptors. The improvement or alteration of unfavourable structural and biological properties of peptide and proteins can be realized by using their mimetics. The design of the protein mimetics is based on the small peptides or non-peptide molecules capable of mimicking the properties or biological activity of a protein owing to the presence of the secondary structure and other features that are analogous to those of the original protein. The determination of the secondary structure properties by using standard spectroscopy methods (IR, NMR and CD spectroscopy) followed with structural-activity relationship study enables the prediction of the biological potential of the protein mimetics.

LEARNING OUTCOMES

1. Explain the disadvantages of the natural peptides (proteolytic instability, polarity, flexibility).
2. Explain the role and usage of the small petide and non-peptide molecules in the design of the peptide helices, sheets and turns.
3. Synthesis and conformational analysis of peptidomimetics by using standard spectroscopic methods (IR, NMR and CD spectroscopy) and prediction of biological potential by comparison of their secondary structures with those of the original peptides.
4. Discuss the potential application of peptidomimetics in biotechnology and food technology.

Lectures

Literature