Biomolecules, Volume 14, Issue 7 (July 2024) – 150 articles
Cover Story (view full-size image):
DMD4B-HYDRA simulations of oligomer formation by naturally occurring Aβ1−38, Aβ1−40, Aβ1−42, and Aβ1−43 reveal that they assemble through distinct oligomer formation pathways. Oligomers of different sizes exhibit self-similarity, yet their structure is isoform specific. While Aβ1−38 and Aβ1−40 hexamers adopt dumb-bell shapes, Aβ1−42 hexamers have a compact C-terminally stabilized core with flexible, solvent-exposed N-termini. Aβ1−42 and Aβ1−43, reported to be neurotoxic, form on average larger oligomers than presumably neuroprotective Aβ1−38 and Aβ1−40. Because larger oligomers are expected to possess an increased affinity to form water-permeable pores in a bilayer, these findings suggest that therapeutic strategies targeting oligomer size reduction will mitigate Aβ-mediated toxicity. View this paper
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