Self-assembly of selenopeptides

Summary: This is a collaborative study involving the aggregation of synthetic peptides derived from the 21st amino acid, i.e., selenocysteine. To our surprise, we observed that seleno-peptides form supramolecular architecture similar to the proteinous aggregates. We demonstrate the first-ever reported self-assembled structures of any selenopetides. The nanoscale structures were found to be amyloid fibrils (doi.org/10.1039/C8CC06528D). In another study, we have reported a completely different class of peptides that self-assembled to a mesoscale tubular aggregate. Despite the broad interest of peptide nanotubes, a limited number of such peptides have been reported till now.  Based on the selenopeptide chemistry, we have demonstrated a new family of peptide-conjugates for such architecture and decipher the importance of Se and the heteroatoms therein (doi.org/10.1021/acsabm.0c01551). A lot to things yet to the deciphered about this new class of selenopeptides which forms different assembled structures- I personally feel happy to be a part at the beginning. We have explored different techniques and designed experiments that are beyond our expertise to understand the system.