Research Projects

The study aims to introduce halogen group and chalcogen motifs through tryptophan modifications in peptide sequences to study their interactions in folded peptides, including short macrocycles, short helices, and foldamers. The researchers will design, synthesize, and introduce these motifs in aromatic amino acids, followed by their incorporation in short and folded peptides and foldamers. They will also synthesize halogen group and chalcogen motifs containing L-Tryptophan for facilitating halogen bonding and chalcogen bonding in short peptides, using model peptide oligomers for macrocyclization. The study will also synthesize model short helices to probe the effect of halo-motifs bearing L-Tryptophan for halogen bonding and chalcogen bonding. This strategy could be used to include halo-motifs at the N-terminus, Mid-terminus, and C-terminus of the helix, providing a generic platform to explore the feasibility of halogen bonding and chalcogen bonding with termini dependence.