Amyloid beta-peptide (A beta) is a major fibrillar component of neuritic plaques in Alzheimer's disease (AD) brains and is related to the pathogenesis of the disease. We hypothesized that amyloid formation could be inhibited by peptides homologous to A beta (position 17-21) with a similar degree of hydrophobicity, but with a very low propensity to adopt a beta-sheet conformation by incorporating proline residues (anti-beta-sheet peptides or beta-sheet inhibitors). An 11-residue peptide with these characteristics binds to A beta, inhibits A beta fibril formation and partially disaggregates preformed fibrils in vitro. Shorter anti-beta-sheet peptides and analogs containing D-amino acids are also able to inhibit A beta fibrillogenesis. The latter are more resistant to proteolytic degradation and may serve as a starting point to design more efficient peptides derivatives to inhibit amyloidogenesis in vivo.
Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation.
C. Soto,M. Kindy,Marc H. Baumann,Blas Frangione
Published 1996 in Biochemical and Biophysical Research Communications - BBRC
ABSTRACT
PUBLICATION RECORD
- Publication year
1996
- Venue
Biochemical and Biophysical Research Communications - BBRC
- Publication date
1996-09-24
- Fields of study
Medicine, Chemistry
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
CITATION MAP
EXTRACTION MAP
CLAIMS
- No claims are published for this paper.
CONCEPTS
- No concepts are published for this paper.
REFERENCES
Showing 1-29 of 29 references · Page 1 of 1