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Heme-peptide/protein interactions: The binding of heme octa and undecapeptides, and microperoxidase-8 and -11, to human serum albumin

1989; Elsevier BV; Volume: 37; Issue: 2 Linguagem: Inglês

10.1016/0162-0134(89)80032-7

1873-3344

Paul A. Adams, Richard D. Goold, Alfred E. Thumser,

Spectroscopy and Quantum Chemical Studies

The interaction of the heme octa (MP-8) and undeca (MP-11) peptides derived from cytochrome c with lipidated human serum albumin (HSA) has been investigated in aqueous solution. It is demonstrated that complex formation occurs in each case with a 1:1 stoichiometry. CN− binding has been used to investigate the accessibility of the heme in each complex by comparison with CN− interaction with methemalbumin. A preliminary study of the kinetics of the Fe3+MP-8/11 human serumalbumin (HSA) interaction demonstrates a clear ligand-size-related effect on mechanism of interaction—an ad hoc explanation of which is given in terms of HSA existing as two nonconverting conformers in solution.