Dehydrophenylalanine (\Delta Phe) as a \beta Breaker:Extended Structure Terminated by a \Delta Phe-Induced Turn in the Pentapeptide Boc-Phe1-Ala2-Ile3-\Delta Phe4-Ala5-OMe

Gupta, Madhvi and Acharya, Rudresh and Mishra, Aseem and Ramakumar, Suryanarayanarao and Ahmed, Faizan and Chauhan, Virander Singh (2008) Dehydrophenylalanine (\Delta Phe) as a \beta Breaker:Extended Structure Terminated by a \Delta Phe-Induced Turn in the Pentapeptide Boc-Phe1-Ala2-Ile3-\Delta Phe4-Ala5-OMe. In: ChemBioChem, 9 (9). pp. 1375-1378.

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Abstract

Amyloid is a highly insoluble, aggregated state of certain polypeptide sequences associated with a range of debilitating diseases.A key step in amyloid formation is the transition of a protein from its native structure to a \beta-sheet arrangement; this suggests that the prevention of the ability of amyloidogenic proteins to adopt a \beta-sheet conformation would be useful as a way to impede the amyloid self-assembly process[1].The use of \beta-breaker residues is one approach for the development of peptide-based fibrillization-inhibiting drugs. Soto et al. demonstrated that the incorporation of \beta-sheet-breaker elements into short peptides composed of the recognition sequence of the amyloidogenic proteins inhibited amyloid formation. In this context, \beta-sheet-breaker residues, such as proline and a-aminoisobutyric acid (Aib), which is an unnatural amino acid residue, have been found to inhibit amyloid fibril formation.$^{[2a-d]}$

Item Type: Journal Article Copyright of this article belongs to John Wiley and Sons. Alzheimer's disease;circular dichroism;dehydrophenylalanine; protein structures;trifluoroethanol Division of Physical & Mathematical Sciences > Physics 18 Jul 2008 24 Feb 2012 06:05 http://eprints.iisc.ernet.in/id/eprint/15088