Mechanistic insights into the mitigation of Aβ aggregation and protofibril destabilization by a<scp>d</scp>-enantiomeric decapeptide rk10
Kamaljot Singh, Anupamjeet Kaur, Deepti Goyal, Bhupesh Goyal
Abstract
MD simulations highlighted that rk10 induces a significant increase in helical and a complete reduction of β–sheet content in Aβ 42 monomer. Remarkably, rk10 destabilized Aβ 42 protofibril by lowering the binding affinity between protofibril chains.
Topics & Concepts
MonomerChemistryEnantiomerBiophysicsStereochemistryCrystallographyOrganic chemistryPolymerBiologyProtein Structure and DynamicsGlycosylation and Glycoproteins ResearchProtein Kinase Regulation and GTPase Signaling