Molecular-level organization of coassembled β-sheet peptide nanofibers
Wong, Kong Ming
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Functional biomaterials that recapitulate the complexity and sophistication of biological systems can be difficult to access given current techniques. One promising route towards building biomaterials with controlled nanoscale organization is coassembling β-sheet peptides. Coassembling β-sheet peptide designs are predominated by the concept of charge complementarity in which the two peptide sequences are modified to include charged amino acids giving rise to either an overall positive or overall negative charge. Electrostatic repulsion prevents self-assembly while attraction between oppositely charged peptides promotes β-sheet assembly. While previous studies have assessed the secondary structure of nanofibers fabricated from charge-complementary peptides, there is no detailed molecular-level description of how these peptides strands arrange within the nanofiber. Consequently, we lack an understanding of how these peptides coassemble and how to design the sequences to form a specific coassembled structure. In this thesis, we investigate the molecular-level organization within coassembling β-sheet peptide nanofibers by a combination of experimental and computational techniques. Results reveal a significant number of structural defects are formed highlighting the challenge in designing coassembling β-sheet peptides and providing insights into future designs.