CPHPC
 | |
| Names | |
|---|---|
| IUPAC name
(2R)-1-[6-[(2R)-2-Carboxypyrrolidin-1-yl]-6-oxohexanoyl]pyrrolidine-2-carboxylic acid | |
| Other names
Ro 63-8695 | |
| Identifiers | |
224624-80-0  | |
| 3D model (Jmol) | Interactive image |
| ChEMBL | ChEMBL25263 |
| ChemSpider | 111662 |
| 8256 | |
| PubChem | 125516 |
| UNII | WO97N24A47 |
| |
| |
| Properties | |
| C16H24N2O6 | |
| Molar mass | 340.37 g/mol |
| Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). | |
verify (what is  ?) | |
| Infobox references | |
CPHPC (R-1-[6-[R-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl] pyrrolidine-2-carboxylic acid) is a proline-derived small molecule able to strip amyloid P (AP) from deposits by reducing levels of circulating serum amyloid P (SAP). The SAP-amyloid association has also been identified as a possible drug target for anti-amyloid therapy, with the recent development and first stage clinical trials of CPHPC for amyloidosis.[1]
CPHPC has also been patented for possible treatment of Alzheimer's disease.[2]
Mechanism
The symmetrical nature of CPHPC allows it to bind to two molecules of AP (the SAP subunits). This allows five molecules of CPHPC to bind two SAP pentamers together by the B/binding face blocking the binding on to existing amyloid deposits.[3]
References
- ↑ Pepys MB, Herbert J, Hutchinson WL, Tennent GA, Lachmann HJ, Gallimore JR, Lovat LB, Bartfai T, Alanine A, Hertel C, Hoffmann T, Jakob-Roetne R, Norcross RD, Kemp JA, Yamamura K, Suzuki M, Taylor GW, Murray S, Thompson D, Purvis A, Kolstoe S, Wood SP, Hawkins PN (2002). "Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis". Nature. 417 (6886): 254–9. doi:10.1038/417254a. PMID 12015594.
- ↑ Pharmaceutical Formulations for the Treatment of Alzheimer's Disease WO 2008014232
- ↑ Reducing the Supply of Amyloid Fibril Precursor Proteins, MedScape Today
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