| Home > Publications database > Structural Impact of N‐terminal Pyroglutamylate in an Amyloid‐β(3‐42) Fibril Probed by Solid‐State NMR Spectroscopy > print |
| 001 | 1021672 | ||
| 005 | 20250204113756.0 | ||
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| 100 | 1 | _ | |a Gardon, Luis |0 P:(DE-Juel1)185029 |b 0 |u fzj |
| 245 | _ | _ | |a Structural Impact of N‐terminal Pyroglutamylate in an Amyloid‐β(3‐42) Fibril Probed by Solid‐State NMR Spectroscopy |
| 260 | _ | _ | |a Weinheim |c 2024 |b Wiley-VCH |
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| 520 | _ | _ | |a Extracellular 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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| 700 | 1 | _ | |a Becker, Nina |0 P:(DE-Juel1)178027 |b 1 |
| 700 | 1 | _ | |a Gremer, Lothar |0 P:(DE-Juel1)145165 |b 2 |e Corresponding author |
| 700 | 1 | _ | |a Heise, Henrike |0 P:(DE-Juel1)132002 |b 3 |e Corresponding author |
| 773 | _ | _ | |a 10.1002/chem.202303007 |g p. e202303007 |0 PERI:(DE-600)1478547-X |n 10 |p e202303007 |t Chemistry - a European journal |v 30 |y 2024 |x 0947-6539 |
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