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001021672 1001_ $$0P:(DE-Juel1)185029$$aGardon, Luis$$b0$$ufzj
001021672 245__ $$aStructural Impact of N‐terminal Pyroglutamylate in an Amyloid‐β(3‐42) Fibril Probed by Solid‐State NMR Spectroscopy
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001021672 520__ $$aExtracellular amyloid-β (Aβ) plaques, primarily formed by Aβ(1-40) and Aβ(1-42) fibrils, are a hallmark of Alzheimer's disease. The Aβ peptide can undergo a high variety of different post-translational modifications including formation of a pyroglutamate (pGlu, pE) at N-terminal Glu3 or Glu11 of truncated Aβ(3-x) or Aβ(11-x), respectively. Here we studied structural similarities and differences between pEAβ(3-42) and LS-shaped Aβ(1-42) fibrils grown under identical conditions (pH 2) using solid-state NMR spectroscopy. We show that the central region of pEAβ(3-42) fibrils including the turn region around V24 is almost identical to Aβ(1-42) showing similar β-strands also at the N-terminus. The missing N-terminal residues D1-A2 along with pE3 formation in pEAβ(3-42) preclude a salt bridge between K28-D1' as in Aβ(1-42) fibrils. G37 and G38 act as highly sensitive internal sensors for the modified N-terminus, which remains rigid over ~five pH units.
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001021672 7001_ $$0P:(DE-Juel1)178027$$aBecker, Nina$$b1
001021672 7001_ $$0P:(DE-Juel1)145165$$aGremer, Lothar$$b2$$eCorresponding author
001021672 7001_ $$0P:(DE-Juel1)132002$$aHeise, Henrike$$b3$$eCorresponding author
001021672 773__ $$0PERI:(DE-600)1478547-X$$a10.1002/chem.202303007$$gp. e202303007$$n10$$pe202303007$$tChemistry - a European journal$$v30$$x0947-6539$$y2024
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