Fluorinated beta-sheet breaker peptides

• Type: Article in International Scientific Journal
• Date: 2014

Authors

Joana A. Loureiro (Author) FEUP; Rosa Crespo (Author) FEUP; Hans Börner (Author) Other; Pedro M. Martins (Author) ICBAS; Fernando A. Rocha (Author) FEUP; Manuel Coelho (Author) FEUP; M. Carmo Pereira (Author) FEUP; Sandra Rocha (Author) Other

Journal

Title: Journal of Materials Chemistry B

Vol. 2 No. 16

Pages: 2259-2264

ISSN: 2050-7518

Publisher: Royal Society of Chemistry

Indexing

ISI Web of Knowledge - 24 Citations

ISI Web of Science

Scopus - 34 Citations

Scientific classification

CORDIS: Technological sciences

FOS: Engineering and technology

Associated Projects

Referência: PTDC/QUI-BIQ/102827/2008 - Concepção de péptidos fluorados para inibição da agregação do péptido beta-amilóide e avaliação da sua actividade biológica

Other information

Authenticus ID: P-009-ASR

DOI: 10.1039/c3tb21483d

Abstract (EN): 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6