Ability of proteins to adopt unique tertiary structures for performing specific biological tasks and regulation of their function through stimuli-induced reversible switching from one conformation to another are fundamental to all cellular processes. (1) The past couple of decades have seen considerable success in the design and synthesis of a large number of oligomeric systems with comparable secondary structures as seen in functional proteins. (2) Apart from their importance in unravelling the basis of bio-molecular structure and function, use of such oligomers as competitive inhibitors of protein-protein interactions (PPIS) is also being actively explored. The main challenge in targeting protein-protein interfaces is the fairly large area of contact (1500-3000 A2) which is usually shallow. Synthetic peptides with conformational complementarity and suitable distribution of donoracceptor sites will be promising in this regard. (3) Peptidomimetics are less sensitive to hydrolysis by cellular proteases and hence show better bioavailability than natural peptides, which make them useful in the design of new therapeutic agents capable of targeting key PPIs that are associated with pathogenesis of different diseases. (4) This seminar will initially discuss the progress made in the design of synthetic peptide oligomers with secondary structural preferences as that of natural systems. Their applications in biology and medicine will also be discussed with suitable examples. With this background, an outline of the proposed doctoral research with objectives, and different classes of peptides selected for synthesis and biological studies will be presented.

References:
1. Wang, Z. A.; Ding, X. Z.; Tian, C. L.; Zheng, J. S., RSC Adv., 2016, 00, 1-9.
2. Gimeno, M. P.; Glas, A.; Koch, O.; Grossmann, T. N., Angew. Chem. Int. Ed., 2015,
54, 8896 – 8927.
3. Lenci, E.; Trabocchi, A., Chem. Soc. Rev., 2020, 49, 3262-3277.
4. Grob, A.; Hashimoto, C.; Sticht, H.; Eichlert, J., FRONT BIOENG BIOTECH., 2016,
3, 211.