Peptide Self-Assembly from the Molecular to the Macroscopic Scale at Standard Conditions
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The second part of the dissertation focuses on the study of self-assembly as a way to make useful peptide-based materials. There are major efforts underway to study protein self-assembly for various medical and industrial reasons. Despite huge progress, most studies have focused on nanoscale self-assembly but the crossover to the macroscopic scale remains a challenge. We show that peptide self-assembly into macroscopic fibers is possible in vitro under physiological conditions. We characterize the fibers and propose a mechanism by which they form. The macroscopic fibers self-assemble from a combination of Î²- and Î±-peptides and are similar to other naturally-occurring systems in which templated self-assembly is used to create functional peptide materials. Finally, the ability to control macroscopic properties of the fiber by varying the ratio of constituent peptides is demonstrated.
Owing to the richness of the amino acid building blocks, peptides are highly versatile structural and functional building blocks. The ability to extend and control peptide self-assembly over multiple length scales is a significant leap toward incorporating peptide materials into dynamic systems of higher complexity and functionality.
- Doctoral Dissertations