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.
P251
NANOPARTICLES
PATHOGENESIS
V47
AMYLOIDOGENICITY
FIBRILLOGENESIS
1978
PROTEIN
ALZHEIMERS-DISEASE
AMYLOID FIBRILS
ANNUAL REVIEW OF BIOCHEMISTRY
SOLID-STATE NMR
OU PY
CONFORMATION
OLIGOMERS
Author
J. A. Loureiro
Universidade do Porto
R. Crespo
Universidade do Porto
H. Borner
Humboldt-Universitat zu Berlin
P. M. Martins
Universidade do Porto
F. A. Rocha
Universidade do Porto
M. A. N. Coelho
Universidade do Porto
M. C. Pereira
Universidade do Porto
Sandra Rocha
Chalmers, Chemical and Biological Engineering, Physical Chemistry
Journal of Materials Chemistry B
20507518 (ISSN) 2050750X (eISSN)
Vol. 2 16 2259-2264Subject Categories (SSIF 2011)
Materials Engineering
Biochemistry and Molecular Biology
DOI
10.1039/c3tb21483d