Fluorinated beta-sheet breaker peptides
Artikel i vetenskaplig tidskrift, 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
Författare
J. A. Loureiro
Universidade do Porto
R. Crespo
Universidade do Porto
H. Borner
Humboldt-Universität 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, Kemi- och bioteknik, Fysikalisk kemi
Journal of Materials Chemistry B
2050750x (ISSN) 20507518 (eISSN)
Vol. 2 16 2259-2264Ämneskategorier
Materialteknik
Biokemi och molekylärbiologi
DOI
10.1039/c3tb21483d