Abstract

The autonomous organization of parts into ordered architectures, or biomolecular self-assembly, is an elementary natural process that defines and guides the construction and function of living organisms. This phenomenon has emerged as a potent tool for the creation of novel biomaterials, with peptide-based instances benefitting from intrinsic modularity, ease of de novo design and synthesis, biocompatibility, and chemical versatility. These properties enable methodical modifications that generate suprastructures with a wide variety of morphologies and functionalities, supporting a broad range of biomedical applications. Further, the chiral nature of amino acids permits synthesis of either left- or right-handed peptides; in recent years, this has advanced from complete D-substitution to the incorporation of both L- and D-residues into ‘heterochiral’ sequences. When peptides consist of multiple identical domains, segmenting chiral inversions according to these repeat units gives rise to ‘block’ heterochirality. Through combinatorial exploration of model cross-β peptides, this work furthers our understanding of chiral patterning and its powerful influence over hierarchical supramolecular assembly.

Committee Chair

Jai Rudra

Degree

Doctor of Philosophy (PhD)

Author's Department

Biomedical Engineering

Author's School

McKelvey School of Engineering

Document Type

Dissertation

Date of Award

12-22-2023

Language

English (en)

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