A buried glutamate in the cross-β core renders β-endorphin fibrils reversible
Yuying Liu, Yu Zhang, Yunxiang Sun, Feng Ding
Abstract
iterative deprotonation of Glu8 and induced structural disruption, all Glu8 residues would be progressively deprotonated. Electrostatic repulsion between deprotonated Glu8 residues along with their high solvation tendency disrupted the hydrogen bonding between the β1 strands and increased the solvent exposure of those otherwise buried residues in the cross-β core. Overall, our computational study reveals that the strategic positioning of ionizable residues into the cross-β core is a potential approach for designing reversible amyloid fibrils as pH-responsive smart bio-nanomaterials.
Topics & Concepts
FibrilDeprotonationGlutamate receptorCore (optical fiber)ChemistryBiophysicsCrystallographyMaterials scienceBiochemistryOrganic chemistryBiologyIonReceptorComposite materialSupramolecular Self-Assembly in MaterialsAlzheimer's disease research and treatmentsLipid Membrane Structure and Behavior