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Fluorinated beta-sheet breaker peptides

J. A. Loureiro ; R. Crespo ; H. Borner ; P. M. Martins ; F. A. Rocha ; M. Coelho ; M. C. Pereira ; Sandra Rocha (Institutionen för kemi- och bioteknik, Fysikalisk kemi)
Journal of Materials Chemistry B (2050-750X). Vol. 2 (2014), 16, p. 2259-2264.
[Artikel, refereegranskad vetenskaplig]

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.

Nyckelord: SOLID-STATE NMR, ALZHEIMERS-DISEASE, AMYLOID FIBRILS, PROTEIN, OLIGOMERS, AMYLOIDOGENICITY, FIBRILLOGENESIS, NANOPARTICLES, CONFORMATION, PATHOGENESIS, OU PY, 1978, ANNUAL REVIEW OF BIOCHEMISTRY, V47, P251



Denna post skapades 2014-05-27. Senast ändrad 2014-10-21.
CPL Pubid: 198642

 

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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Fysikalisk kemi (2005-2014)

Ämnesområden

Biokemi och molekylärbiologi
Materialteknik

Chalmers infrastruktur