The article explores the design of tunable biomaterials based on supramolecular chirality, particularly focusing on the amyloid-β 42 peptide, which is implicated in neurodegenerative diseases. The authors investigate how sequence modifications can regulate the supramolecular chirality of amyloid assemblies, which can be either left-handed or right-handed. They find that C-terminal modifications can tune the energy barrier for chiral inversion, allowing for temperature-triggered changes in chirality. This property is leveraged to design peptides that can release anticancer drugs in response to temperature changes, demonstrating a potential therapeutic approach for regulating amyloid morphology in neurodegenerative diseases. The study provides insights into the general principles of controlling supramolecular chirality and suggests applications in drug delivery and other fields.The article explores the design of tunable biomaterials based on supramolecular chirality, particularly focusing on the amyloid-β 42 peptide, which is implicated in neurodegenerative diseases. The authors investigate how sequence modifications can regulate the supramolecular chirality of amyloid assemblies, which can be either left-handed or right-handed. They find that C-terminal modifications can tune the energy barrier for chiral inversion, allowing for temperature-triggered changes in chirality. This property is leveraged to design peptides that can release anticancer drugs in response to temperature changes, demonstrating a potential therapeutic approach for regulating amyloid morphology in neurodegenerative diseases. The study provides insights into the general principles of controlling supramolecular chirality and suggests applications in drug delivery and other fields.