Fluorinated beta-sheet breaker peptides
Journal article, 2014
The aggregation of amyloid-beta peptide (Ab) has been linked to the formation of neuritic plaques, which are pathological hallmarks of Alzheimer's disease. We synthesized peptides containing fluorinated amino acids and studied their effect on the Ab aggregation. The peptides were based on the sequence LVFFD, in which valine was substituted by either 4,4,4-trifluorovaline or 4-fluoroproline, or the phenylalanine at position 3 was replaced by 3,4,5-trifluorophenylalanine. Our results demonstrate that fluorination of the hydrophobic residue valine or phenylalanine is effective in preventing the Ab aggregation. This study opens up the possibility of using new sequences based on fluorinated amino acids to inhibit the amyloid- fibril formation.
1978
ANNUAL REVIEW OF BIOCHEMISTRY
P251
NANOPARTICLES
OU PY
V47
ALZHEIMERS-DISEASE
PATHOGENESIS
AMYLOIDOGENICITY
SOLID-STATE NMR
PROTEIN
CONFORMATION
AMYLOID FIBRILS
FIBRILLOGENESIS
OLIGOMERS
Author
J. A. Loureiro
University of Porto
R. Crespo
University of Porto
H. Borner
Humboldt University of Berlin
P. M. Martins
University of Porto
F. A. Rocha
University of Porto
M. A. N. Coelho
University of Porto
M. C. Pereira
University of Porto
Sandra Rocha
Chalmers, Chemical and Biological Engineering, Physical Chemistry
Journal of Materials Chemistry B
2050750x (ISSN) 20507518 (eISSN)
Vol. 2 16 2259-2264Subject Categories
Materials Engineering
Biochemistry and Molecular Biology
DOI
10.1039/c3tb21483d