Photocontrolled Reversible Amyloid Fibril Formation of Parathyroid Hormone-Derived Peptides.

ABSTRACT: Peptide fibrillization is crucial in biological processes such as amyloid-related diseases and hormone storage, involving complex transitions between folded, unfolded, and aggregated states. We here employ light to induce reversible transitions between aggregated and nonaggregated states of a peptide, linked to the parathyroid hormone (PTH). The artificial light-switch 3-{[(4-aminomethyl)phenyl]diazenyl}benzoic acid (AMPB) is embedded into a segment of PTH, the peptide PTH_25-37, to control aggregation, revealing position-dependent effects. Through in silico design, synthesis, and experimental validation of 11 novel PTH_25-37-derived peptides, we predict and confirm the amyloid-forming capabilities of the AMPB-containing peptides. Quantum-chemical studies shed li

SUBMITTER: Paschold A 

PROVIDER: S-EPMC11261605 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature