Inhibitor and substrate cooperate to inhibit amyloid fibril elongation of α-synuclein
Emil Dandanell Agerschou, Vera Borgmann, Michael M. Wördehoff, Wolfgang Hoyer
Abstract
, wild-type αS, supports inhibition by stabilizing the elongation-incompetent blocked state. This observation allowed us to create inhibitor-substrate fusions that achieved inhibition at low nanomolar concentration. We conclude that inhibitor-substrate cooperativity can be exploited for the design of fibril growth inhibitors.
Topics & Concepts
FibrilElongationMonomerAmyloid fibrilChemistryBiophysicsSubstrate (aquarium)Amyloid (mycology)BiochemistryAmyloid βMaterials scienceBiologyPolymerMedicineUltimate tensile strengthPathologyDiseaseMetallurgyInorganic chemistryOrganic chemistryEcologyParkinson's Disease Mechanisms and TreatmentsAlzheimer's disease research and treatmentsbiodegradable polymer synthesis and properties