Peptide Self-Assembly into Amyloid Fibrils: Unbiased All-Atom Simulations

Bradley L. Nilsson, Gizem Celebi Torabfam, Cristiano L. Dias

Research output: Contribution to journalReview articlepeer-review

Abstract

Protein self-assembly plays an important role in biological systems, accounting for the formation of mesoscopic structures that can be highly symmetric as in the capsid of viruses or disordered as in molecular condensates or exhibit a one-dimensional fibrillar morphology as in amyloid fibrils. Deposits of the latter in tissues of individuals with degenerative diseases like Alzheimer’s and Parkinson’s has motivated extensive efforts to understand the sequence of molecular events accounting for their formation. These studies aim to identify on-pathway intermediates that may be the targets for therapeutic intervention. This detailed knowledge of fibril formation remains obscure, in part due to challenges with experimental analyses of these processes. However, important progress is being achieved for short amyloid peptides due to advances in our ability to perform completely unbiased all-atom simulations of the self-assembly process. This perspective discusses recent developments, their implications, and the hurdles that still need to be overcome to further advance the field.

Original languageEnglish (US)
Pages (from-to)3320-3328
Number of pages9
JournalJournal of Physical Chemistry B
Volume128
Issue number14
DOIs
StatePublished - Apr 11 2024

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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