Abstract
Investigating amyloid nanofibril self-assembly, with an emphasis on the electromechanical property of amyloid peptides, namely, piezoelectricity, may have several important implications: 1) the self-assembly process can hinder the biological stability and give rise to the formation of amyloid structures associated with neurodegenerative diseases; 2) investigations in this field may lead to an improved understanding of high-performance, functional biological nanomaterials, 3) new technologies could be established based on peptide self-assembly and the resultant functional properties, e.g., in the creation of a piezoelectric device formed with vertical diphenylalanine peptide tubes as a piezoelectric biosensor, and 4) new knowledge can be generated about neurodegenerative disorders, potentially yielding new therapies. Therefore, in this review, we will present the current investigations associated with self-assembly of amyloid-beta, the mechanisms that generate new structures, as well as theoretical calculations exploring the functionality of the structures under physiological pressure and electric field.
Highlights
Investigating amyloid nanofibril self-assembly, with an emphasis on the electromechanical property of amyloid peptides, namely, piezoelectricity, may have several important implications: 1) the self-assembly process can hinder the biological stability and give rise to the formation of amyloid structures associated with neurodegenerative diseases; 2) investigations in this field may lead to an improved understanding of high-performance, functional biological nanomaterials, 3) new technologies could be established based on peptide self-assembly and the resultant functional properties, e.g., in the creation of a piezoelectric device formed with vertical diphenylalanine peptide tubes as a piezoelectric biosensor, and 4) new knowledge can be generated about neurodegenerative disorders, potentially yielding new therapies
Modifications to the self-assembly properties or molecular stability of amyloids [3] can result in the formation of amyloid fibrils that completes the self-assembly process in the cell membrane [3] [4]
In the study of the cause of neurodegenerative disorders, several approaches can be established, such as assembling the amyloids with lipids, since other neuronal factors change with the presence of amyloids, as has been discovered for soluble fractions of lipids or potassium voltage-gated channels [5]; additional experiments showed a change in the aggregation of the amyloid molecules when interacting with other biomacromolecules
Summary
In the study of the cause of neurodegenerative disorders, several approaches can be established, such as assembling the amyloids with lipids, since other neuronal factors change with the presence of amyloids, as has been discovered for soluble fractions of lipids or potassium voltage-gated channels [5]; additional experiments showed a change in the aggregation of the amyloid molecules when interacting with other biomacromolecules. These observations, for instance, indirectly show that lipids and voltage-sensitive peptides modify the structural and aggregation properties of the amyloids. In order to define the role of the external factors on the assembly of amyloids, it is necessary to study the electromechanical properties as tunable features in the amyloids
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