Design strategies for anti-amyloid agents

Jody M. Mason, Nicoleta Kokkoni, Kelvin Stott, Andrew J. Doig

    Research output: Contribution to journalArticlepeer-review


    Numerous diseases have been linked to a common pathogenic process called amyloidosis, whereby proteins or peptides clump together in the brain or body to form toxic soluble oligomers and/or insoluble fibres. An attractive strategy to develop therapies for these diseases is therefore to inhibit or reverse protein/peptide aggregation. A diverse range of small organic ligands have been found to act as aggregation inhibitors. Alternatively, the wild-type peptide can be derivatised so that it still binds to the amyloid target, but prevents further aggregation. This can be achieved by adding a bulky group or charged amino acid to either end of the peptide, or by incorporating proline residues or N-methylated amide groups.
    Original languageEnglish
    Pages (from-to)526-532
    Number of pages6
    JournalCurrent Opinion in Structural Biology
    Issue number4
    Publication statusPublished - 1 Aug 2003


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