Compact fibril-like structure of amyloid β-peptide (1-42) monomers

Bogdan Barz*, Alexander K. Buell, Soumav Nath

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Amyloid β (Aβ) monomers are the smallest assembly units, and play an important role in most of the individual processes involved in amyloid fibril formation. An important question is whether the monomer can adopt transient fibril-like conformations in solution. Here we use enhanced sampling simulations to study the Aβ42 monomer structural flexibility. We show that the monomer frequently adopts conformations with the N-terminus region structured very similarly to the conformation it adopts inside the fibril. This intrinsic propensity of monomeric Aβ to adopt fibril-like conformations could explain the low free energy barrier for Aβ42 fibril elongation.
Original languageEnglish
JournalChemical Communications
Volume57
Pages (from-to)947-950
Number of pages4
ISSN1359-7345
DOIs
Publication statusPublished - 2021

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