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Binding of Nickel(Ii) and Copper(Ii) to the N-Terminal Sequence of Human Protamine Hp2

  1. Author:
    Bal, W.
    Jezowskabojczuk, M.
    Kasprzak, K. S.

  2. Author Address

    Kasprzak KS NCI FREDERICK CANC RES & DEV CTR COMPARAT CARCINOGENESIS LAB BLDG 538 RM 205 FREDERICK, MD 21702 USA NCI FREDERICK CANC RES & DEV CTR COMPARAT CARCINOGENESIS LAB FREDERICK, MD 21702 USA UNIV WROCLAW FAC CHEM PL-50138 WROCLAW POLAND
    1. Year: 1997
  2. Journal: Chemical Research in Toxicology
    1. 10
    2. 8
    3. Pages: 906-914
  4. Type of Article: Article
  1. Abstract:

    A potentiometric and spectroscopic (UV/vis and CD) study of Cu(II) and Ni(II) binding to the N-terminal pentadecapeptide of human protamine HP2 (HP2(1-15)) was performed. The results indicate that the N-terminal tripeptide motif Arg-Thr-His is the exclusive binding site for both metal ions at a metal to HP2(1-15) molar ratio not higher than 1. The very high value of protonation-corrected stability constant (log *K) for Ni(II)-HP2(1-15) complex, -19,29, indicates that HP2 has the potential to sequester Ni(II) from other peptide and protein carriers, including albumin, The same is likely for Cu(II) (log *K = -13.13). The CD spectra of Cu(II) and Ni(II) complexes of HP2(1-15) indicate that the N-terminal metal binding affects the overall conformation of the peptide that, in turn, may alter interaction of HP2 with DNA. These results imply HP2 as a likely target for the toxic metals Ni(II) and Cu(IT). [References: 50]

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  2. DOI: 10.1021/tx970028x
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