Carnosine inhibits Abeta42 aggregation by perturbing the H-bond network in and around the central hydrophobic cluster
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Amyloid-beta 42 aggregation by scanning force microscopy, circular dichroism and thioflavin T assays; molecular dynamics simulations (0.2 ms cumulative sampling); NMR with a non-aggregating fragment.
What the authors reported
Carnosine slowed amyloid growth without changing the peptide's conformation. Simulations suggested transient contacts with the central hydrophobic cluster, and NMR found no specific binding to a non-aggregating fragment (Abeta 12-28). The authors report that carnosine nonetheless interfered with the peptide's local tendency to form backbone hydrogen bonds near that cluster, and suggest this may block the path to toxic aggregates.
Limits of this study
Cell-free study. Full text not read.
Source
PubMed 23440928 · doi:10.1002/cbic.201200704
Entry checked against PubMed abstract (E-utilities) on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.