TY - JOUR
T1 - Design strategies for anti-amyloid agents
AU - Mason, Jody M
AU - Kokkoni, Nicoleta
AU - Stott, Kelvin
AU - Doig, Andrew J
PY - 2003/8/1
Y1 - 2003/8/1
N2 - 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.
AB - 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.
UR - http://dx.doi.org/10.1016/S0959-440X(03)00100-3
U2 - 10.1016/S0959-440X(03)00100-3
DO - 10.1016/S0959-440X(03)00100-3
M3 - Article
SN - 0959-440X
VL - 13
SP - 526
EP - 532
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 4
ER -