Date of Award
12-22-2023
Degree Name
Doctor of Philosophy (PhD)
Degree Type
Dissertation
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.
Language
English (en)
Chair
Jai Rudra