Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Pepys, M.B. et al.

Pepys, Herbert, Hutchinson, Tennent, Lachmann, Gallimore, Lovat, Bartfai, Alanine, Hertel, Hoffmann, Jakob-Roetne, Norcross, Kemp, Yamamura, Suzuki, Taylor, Murray, Thompson, Purvis, Kolstoe, Wood, Hawkins,

Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis.

The normal plasma protein serum amyloid P component (SAP) binds to fibrils in all types of amyloid deposits, and contributes to the pathogenesis of amyloidosis. In order to intervene in this process we have developed a drug, R-1-[6-[R-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl]pyrrolidine-2-carboxylic acid, that is a competitive inhibitor of SAP binding to amyloid fibrils. This palindromic compound also crosslinks and dimerizes SAP molecules, leading to their very rapid clearance by the liver, and thus produces a marked depletion of circulating human SAP. This mechanism of drug action potently removes SAP from human amyloid deposits in the tissues and may provide a new therapeutic approach to both systemic amyloidosis and diseases associated with local amyloid, including Alzheimer's disease and type 2 diabetes.[1]

References

Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. Pepys, M.B., Herbert, J., Hutchinson, W.L., Tennent, G.A., Lachmann, H.J., Gallimore, J.R., Lovat, L.B., Bartfai, T., Alanine, A., Hertel, C., Hoffmann, T., Jakob-Roetne, R., Norcross, R.D., Kemp, J.A., Yamamura, K., Suzuki, M., Taylor, G.W., Murray, S., Thompson, D., Purvis, A., Kolstoe, S., Wood, S.P., Hawkins, P.N. Nature (2002) [Pubmed]

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