Premium
p3 peptide, a truncated form of Aβ devoid of synaptotoxic effect, does not assemble into soluble oligomers
Author(s) -
Dulin Fabienne,
Léveillé Frédéric,
Ortega Javier Becerril,
Mor Jean-Paul,
Buisson Alain,
Callebaut Isabelle,
Colloc'h Nathalie
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.05.002
Subject(s) - peptide , chemistry , biophysics , oligomer , function (biology) , sequence (biology) , biochemistry , biology , microbiology and biotechnology , polymer chemistry
In previously proposed models of Aβ soluble oligomers, the N‐terminal domain Aβ 1–16 , which is missing in p3 peptides, protects the hydrophobic core of the oligomers from the solvent. Without this N‐terminal part, oligomers of p3 peptides would likely expose hydrophobic residues to water and would consequently be less stable. We thus suggest, based on theoretical and experimental results, that p3 peptides would have a low propensity to assemble into stable oligomers, evolving then directly to fibrillar aggregates. These properties may explain why p3 would be devoid of any impact on synaptic function and moreover, strengthen the hypothesis that Aβ oligomers are the principal synaptotoxic forms of Aβ peptides in Alzheimer disease.