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. 2023 May 1;32(5):e4639. doi: 10.1002/pro.4639

TABLE 1.

Brain‐derived versus synthetic Aβ fibrils.

Brain‐derived Aβ fibrils In vitro synthetic Aβ fibrils
Fibrillar structural polymorphism

  • Aβ1–40: Threefold symmetry of isotopically labeled brain‐seeded Aβ1–40 fibrils as revealed by ssNMR and EM (PDB 2M4J) a (Lu et al., 2013; Paravastu et al., 2009)

  • Aβ1–40: Twofold symmetry of brain‐derived cortical Aβ1–40 fibrils with slightly left‐handed twist as revealed by Cryo‐EM (PDB 6W0O) (Ghosh, Thurber, et al., 2021)

  • Aβ1–40: Twofold symmetry of brain‐derived meningeal Aβ1–40 fibril with twisted right‐handed as revealed by Cryo‐EM (PDB 6SHS) (Kollmer et al., 2019)

  • Aβ1–42: Twofold symmetry of brain‐derived cortical Aβ1–42 fibril with twisted left‐handed as revealed by Cryo‐EM (type I: PDB 7Q4B) (Y. Yang et al., 2022)

  • Aβ1–42: Twofold symmetry of brain‐derived cortical Aβ1–42 fibril with twisted left‐handed as revealed by Cryo‐EM (type II: 7Q4M) (Y. Yang et al., 2022)

  • Aβ1–42: Twofold symmetry of fibrils (Colvin et al., 2016; Wälti et al., 2016; Xiao et al., 2015)

  • Aβ1–40: Twofold (striated ribbon) and threefold (periodically twisted) symmetries of fibrils (Hu et al., 2019; Paravastu et al., 2008; Petkova et al., 2006)
Proteinase K treatment More resistance to proteinase K (Kollmer et al., 2019) Less resistance to proteinase K (Kollmer et al., 2019)
Aβ post‐translational modifications High diversity of post‐translational modifications especially in N‐terminal and C‐terminal truncations. (Arai et al., 1999; Cabrera et al., 2018; Güntert et al., 2006; Kummer & Heneka, 2014; Milton, 2001; Rijal Upadhaya et al., 2014; Rostagno et al., 2018; Sergeant et al., 2003; Wildburger et al., 2017) No diversity in N‐terminal and C‐terminal truncations
Toxicity of Aβ oligomers Higher neurotoxicity (Brody & Gross, 2014; Hong et al., 2018; Jin et al., 2011; Noguchi et al., 2009; Sideris et al., 2021) Lower neurotoxicity (Brody & Gross, 2014; Jin et al., 2011)
a

Structural calculations were performed to accurately determine the fibril structure of Aβ1–40 that is fully consistent with the experimental data (Lu et al., 2013; Miller et al., 2011).