Protein Aggregation in a Nutshell: The Splendid Molecular Architecture of the Dreaded Amyloid Fibrils

Author(s): Dániel Horváth, Dóra K. Menyhárd, András Perczel*.

Journal Name: Current Protein & Peptide Science

Volume 20 , Issue 11 , 2019

Become EABM
Become Reviewer

Graphical Abstract:


The recent high-resolution structures of amyloid fibrils show that the organization of peptide segments into amyloid aggregate architecture is a general process, though the morphology is more complex and intricate than suspected previously. The amyloid fibrils are often cytotoxic, accumulating as intracellular inclusions or extracellular plaques and have the ability to interfere with cellular physiology causing various cellular malfunctions. At the same time, the highly ordered amyloid structures also present an opportunity for nature to store and protect peptide chains under extreme conditions – something that might be used for designing storage, formulation, and delivery of protein medications or for contriving bio-similar materials of great resistance or structure-ordering capacity. Here we summarize amyloid characteristics; discussing the basic morphologies, sequential requirements and 3D-structure that are required for the understanding of this newly (re)discovered protein structure – a prerequisite for developing either inhibitors or promoters of amyloid-forming processes

Keywords: Aggregation, amylogenic peptides, amyloid, amyloid structure, β-sheet, cryo-EM, sequential pattern, ssNMR.

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2019
Page: [1077 - 1088]
Pages: 12
DOI: 10.2174/1389203720666190925102832
Price: $58

Article Metrics

PDF: 10