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Mixing Aβ(1-40) and Aβ(1-42) peptides generates unique amyloid fibrils.

Cerofolini L, Ravera E, Bologna S, Wiglenda T, Böddrich A, Purfürst B, Benilova I, Korsak M, Gallo G, Rizzo D, Gonnelli L, Fragai M, De Strooper B, Wanker EE, Luchinat C
Chem Commun (Camb) 56 8830-8833 (2020)
Related entries: 6ti6, 6ti7

Cited: 19 times
EuropePMC logo PMID: 32749391

Abstract

Recent structural studies show distinct morphologies for the fibrils of Aβ(1-42) and Aβ(1-40), which are believed not to co-fibrillize. We describe here a novel, structurally-uniform 1 : 1 mixed fibrillar species, which differs from both pure fibrils. It forms preferentially even when Aβ(1-42) : Aβ(1-40) peptides are mixed in a non-stoichiometric ratio.

Reviews - 6ti5 mentioned but not cited (1)

  1. Amyloid Cross-Seeding: Mechanism, Implication, and Inhibition. Subedi S, Sasidharan S, Nag N, Saudagar P, Tripathi T. Molecules 27 1776 (2022)

Articles - 6ti5 mentioned but not cited (7)

  1. A lowly populated, transient β-sheet structure in monomeric Aβ1-42 identified by multinuclear NMR of chemical denaturation. Kakeshpour T, Ramanujam V, Barnes CA, Shen Y, Ying J, Bax A. Biophys Chem 270 106531 (2021)
  2. Protein Amyloid Cofactors: Charged Side-Chain Arrays Meet Their Match? Lewkowicz E, Jayaraman S, Gursky O. Trends Biochem Sci 46 626-629 (2021)
  3. Binding Sites of a Positron Emission Tomography Imaging Agent in Alzheimer's β-Amyloid Fibrils Studied Using 19F Solid-State NMR. Duan P, Chen KJ, Wijegunawardena G, Dregni AJ, Wang HK, Wu H, Hong M. J Am Chem Soc 144 1416-1430 (2022)
  4. Characterizing Heparin Tetrasaccharides Binding to Amyloid-Beta Peptide. Zhou X, Wang Y, Zheng W, Deng G, Wang F, Jin L. Front Mol Biosci 9 824146 (2022)
  5. Effect of Date Palm (Phoenix dactylifera) Phytochemicals on Aβ1-40 Amyloid Formation: An in-silico Analysis. Zia Q, Rehman MT, Hashmi MA, Siddiqui S, Bin Dukhyil A, Ahmed MZ, Jamal A, Banawas S, Almalki SG, Owais M, Aldhafeeri HQ, Ibrahim IM, Alturaiki W, AlAjmi MF, Alsieni M, Alqurashi YE. Front Neurosci 16 915122 (2022)
  6. Integrative modeling of diverse protein-peptide systems using CABS-dock. Puławski W, Koliński A, Koliński M. PLoS Comput Biol 19 e1011275 (2023)
  7. Fibrillization Process of Human Amyloid-Beta Protein (1-40) under a Molecular Crowding Environment Mimicking the Interior of Living Cells Using Cell Debris. Hirai M, Arai S, Iwase H. Molecules 28 6555 (2023)


Reviews citing this publication (2)

  1. Interpretable artificial intelligence and exascale molecular dynamics simulations to reveal kinetics: Applications to Alzheimer's disease. Martin W, Sheynkman G, Lightstone FC, Nussinov R, Cheng F. Curr Opin Struct Biol 72 103-113 (2022)
  2. Retinal Alterations Predict Early Prodromal Signs of Neurodegenerative Disease. Casciano F, Zauli E, Celeghini C, Caruso L, Gonelli A, Zauli G, Pignatelli A. Int J Mol Sci 25 1689 (2024)

Articles citing this publication (9)

  1. Alzheimer's Aβ42 and Aβ40 form mixed oligomers with direct molecular interactions. Gu L, Guo Z. Biochem Biophys Res Commun 534 292-296 (2021)
  2. Insights into Cerebral Amyloid Angiopathy Type 1 and Type 2 from Comparisons of the Fibrillar Assembly and Stability of the Aβ40-Iowa and Aβ40-Dutch Peptides. Rajpoot J, Crooks EJ, Irizarry BA, Amundson A, Van Nostrand WE, Smith SO. Biochemistry 61 1181-1198 (2022)
  3. Cryo-EM of Aβ fibrils from mouse models find tg-APPArcSwe fibrils resemble those found in patients with sporadic Alzheimer's disease. Zielinski M, Peralta Reyes FS, Gremer L, Schemmert S, Frieg B, Schäfer LU, Willuweit A, Donner L, Elvers M, Nilsson LNG, Syvänen S, Sehlin D, Ingelsson M, Willbold D, Schröder GF. Nat Neurosci 26 2073-2080 (2023)
  4. Sticker-and-spacer model for amyloid beta condensation and fibrillation. Connor JP, Quinn SD, Schaefer C. Front Mol Neurosci 15 962526 (2022)
  5. A common pathway for detergent-assisted oligomerization of Aβ42. Muhammedkutty FNK, Prasad R, Gao Y, Sudarshan TR, Robang AS, Watzlawik JO, Rosenberry TL, Paravastu AK, Zhou HX. Commun Biol 6 1184 (2023)
  6. Acetylcholine hydrolytic activity of fibrillated β-amyloid (1-40) peptide. Sanchis I, Spinelli R, Siano A. Amino Acids 55 1991-1997 (2023)
  7. Amyposomes, a nanotechnological chaperone with anti-amyloidogenic activity. Re F, Giorgetti S, Biondi B, Scapin S, Mantegazza F, Cassina V, Sesana SM, Rizzi L, Eberini I, Palazzolo L, Beeg M, Gobbi M, Sardina M, Masserini M. Ann Med 55 2205659 (2023)
  8. Heterotypic Interactions between the 40- and 42-Residue Isoforms of β-Amyloid Peptides on Lipid Bilayer Surfaces. Qiang W, Kengwerere MK, Zhao W, Scott FJ, Wutoh-Hughes X, Wang T, Mentink-Vigier F. ACS Chem Neurosci 14 4153-4162 (2023)
  9. The N-Terminal Domain of Aβ40-Amyloid Fibril: The MOMD Perspective of its Dynamic Structure from NMR Lineshape Analysis. Meirovitch E, Liang Z, Freed JH. J Phys Chem B 126 1202-1211 (2022)


Related citations provided by authors (1)

  1. A new structural model of Aβ40 fibrils.. Bertini I, Gonnelli L, Luchinat C, Mao J, Nesi A J Am Chem Soc 133 16013-22 (2011)

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