Electrostatic Complementarity Drives Amyloid/Nucleic Acid Co‐Assembly

Proteinaceous plaques associated with neurodegenerative diseases contain many biopolymers including the polyanions glycosaminoglycans and nucleic acids. Polyanion‐induced amyloid fibrillation has been implicated in disease etiology, but structural models for amyloid/nucleic acid co‐assemblies remain...

Full description

Saved in:
Bibliographic Details
Published in:Angewandte Chemie International Edition 2020-01, Vol.59 (1), p.358-363
Main Authors: Rha, Allisandra K., Das, Dibyendu, Taran, Olga, Ke, Yonggang, Mehta, Anil K., Lynn, David G.
Format: Article
Language:English
Subjects:
Acids
Alzheimer's disease
Amyloid - chemistry
Assembly
Biopolymers
Complementarity
Etiology
Fibrillation
Glycosaminoglycans
Humans
Models, Molecular
Neurodegenerative diseases
nucleic acid/amyloid co-assembly
Nucleic acids
Peptide Nucleic Acids - chemistry
Peptides
Plaques
Polyanions
Polyelectrolytes
solid-state NMR spectroscopy
Static Electricity
Structural models
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Proteinaceous plaques associated with neurodegenerative diseases contain many biopolymers including the polyanions glycosaminoglycans and nucleic acids. Polyanion‐induced amyloid fibrillation has been implicated in disease etiology, but structural models for amyloid/nucleic acid co‐assemblies remain limited. Here we constrain nucleic acid/peptide interactions with model peptides that exploit electrostatic complementarity and define a novel amyloid/nucleic acid co‐assembly. The structure provides a model for nucleic acid/amyloid co‐assembly as well as insight into the energetic determinants involved in templating amyloid assembly. Nucleic acids template amyloid assembly through electrostatic interactions. Structural insights indicate that these dynamic and complementary electrostatic interactions could play a role in the development of pathological lesions, bionanomaterials, and ribonucleoprotein granules.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201907661