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

20507518 (ISSN) 2050750X (eISSN)

Vol. 2 16 2259-2264

Ämneskategorier

Materialteknik

Biokemi och molekylärbiologi

DOI

10.1039/c3tb21483d