The exo-chirality of the α-helix and its implications in peptide self-assembly

Abstract

The alpha-helix has an unexplored potential to draw a second layer of chirality encoded in the order of the primary sequence. In this thesis, we have empirically and computationally demonstrated the existence of exo-helical architectures arising from the first six periodic repetition patterns i, i +x, x = 2-7 in the sequence. A systematic study using a non-canonical chromophore residue with different spacer lengths revealed that a high exo-helix consistency is required to induce ordered coiled coils. Finally, we have also demonstrated for the first time that non-canonical exo-helical patterns can build coiled-coil structures. This study offers a novel perspective in the design of protein-based materials with promising structural and functional features.