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Interaction of serum amyloid P component with hexanoyl bis(D-proline) (CPHPC).

Simon E Kolstoe1, Michelle C Jenvey2, Alan Purvis3

  • 1Laboratory of Protein Crystallography, Wolfson Drug Discovery Unit, Centre for Amyloidosis and Acute Phase Proteins, Division of Medicine (Royal Free Campus), University College London, Rowland Hill Street, London NW3 2PF, England.

Acta Crystallographica. Section D, Biological Crystallography
|August 2, 2014
PubMed
Summary

Serum amyloid P component (SAP) binds CPHPC, forming a complex cleared by the liver. X-ray analysis reveals detailed interactions, aiding CPHPC development for amyloidosis treatment.

Keywords:
CPHPCamyloidosisserum amyloid P component

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Pharmacology

Background:

  • Serum amyloid P component (SAP) is a pentameric human plasma protein.
  • SAP interacts with bivalent ligands like CPHPC via D-proline groups in a calcium-dependent manner.
  • Ligand binding leads to cooperative effects, enhancing affinity and forming stabilized decameric complexes.

Purpose of the Study:

  • To elucidate the high-resolution structural details of the SAP-CPPHC interaction using X-ray crystallography with cadmium ions.
  • To compare the conformational states of CPHPC in solution and when bound to SAP.
  • To inform the therapeutic development of CPHPC for SAP depletion in amyloidosis.

Main Methods:

  • X-ray crystallography of the SAP-CPPHC-cadmium complex.
  • High-performance liquid chromatography (HPLC) for conformational analysis in solution.
  • Comparison of X-ray data with solution-state data.

Main Results:

  • Cadmium-mediated X-ray analysis provided higher resolution structural insights into the SAP-CPPHC interaction compared to calcium.
  • Conformational isomers of CPHPC were identified in solution and in the protein-bound state.
  • The study detailed the specific interactions and conformational preferences of CPHPC when bound to SAP.

Conclusions:

  • High-resolution structural data of the SAP-CPPHC complex enhances understanding of ligand-protein interactions.
  • Understanding CPHPC conformation is crucial for optimizing its efficacy in SAP depletion therapies.
  • The findings support the continued development of CPHPC for treating amyloidosis and related conditions.