Interaction of heme with a synthetic peptide mimicking the putative heme-binding site of histidine-rich glycoprotein.

We synthesized a hexapeptide, Gly-His-His-Pro-His-Gly, previously identified as a tandem motif in the histidine-rich glycoprotein (HRG) which has multiple heme-binding sites. Binding of heme to the peptide was demonstrated by the characteristic difference spectrum showing a close resemblance to that of HRG, implying that the peptide binds heme through biaxial coordination with histidine imidazoles. Furthermore, the EPR spectra of the heme-peptide and heme-HRG complexes were almost completely identical in pattern, showing signals characteristic of the low spin iron. The results suggest that the synthetic peptide simulates the heme-binding properties of HRG and that each tandem motif in HRG serves as a unitary binding site for heme.