Abstract
Peptide-based materials have attracted considerable attention as therapeutic agents and biomaterials owing to their excellent biocompatibility, structural versatility, and ability to self-assemble into functional supramolecular architectures. However, the molecular principles governing peptide self-assembly and their relationships with biological function remain incompletely understood, limiting the rational design of peptide-based materials. This thesis investigates peptide self-assembly through the design and characterization of diverse peptide systems, including intrinsically disordered peptide (IDP)-derived sequences, enzyme-responsive peptides, and peptide–porphyrin conjugates. By combining rational molecular design with structural, spectroscopic, and biological characterization, this work demonstrates how subtle variations in peptide sequence, chirality, and molecular conjugation regulate intermolecular interactions, assembly pathways, and resulting nanostructures. Collectively, this work provides molecular insights into the mechanisms of peptide self-assembly and demonstrates how controlling supramolecular organization can be used to tune biological activity and material function. These findings establish general design principles for developing peptide-based biomaterials with programmable structures and emerging biomedical applications.