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Impact of the peptide sequence on the coordination abilities of albumin-like tripeptides towards Cu2+, Ni2+ and Zn2+ ions. Potential albumin-like peptide chelators.
Autorzy
Rok wydania
2002
Czasopismo
Numer woluminu
26
Strony
264-268
DOI
10.1039/B107412C
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
Thermodynamic and spectroscopic studies have shown that the insertion of α-hydroxylmethylserine (HmS) residues into the N-terminal peptide motif of human serum albumin results in a very powerful chelating agent for Cu2+ and Ni2+ ions. The insertion of two HmS residues results in the HmS–HmS–His–OH/NH2 sequence, which is the most effective chelating agent based on an albumin-like sequence for both studied metal ions, especially when the C-terminal carboxylate is protected by an amide function.Our recent studies on the binding ability of the peptides containing α-hydroxymethylserine (HmS)1–4 have shown that insertion of this residue into the peptide sequences significantly increases the stability of their complexes with Cu2+, Ni2+ and Zn2+ ions. Although the basicity of the aminonitrogen of HmS is distinctly lower than that of the other amino acid residues, the insertion of its nitrogen into the peptide bond enhances the π-electron contribution to the metal–nitrogen bond. As a consequence, a considerable increase in the stability of the formed complexes is observed.4 The results reported recently have shown that insertion of two α-hydroxymethylserine residues in an N-terminal albumin-like sequence leads to the most effective peptide chelating agent for Cu2+ and Ni2+ ions.4 The albumin-like sequence is one of the basic structures used in metal ion binding, not only by albumin species but also by several other proteins.5 This inspired us to undertake systematic studies on the co-ordination ability of oligopeptides having a histydyl residue in the third position and various amino acid residues at its N-terminal side, including that of the human serum albumin sequence, Asp–Ala–His–OH/NH2. Tripeptides with an unprotected C-terminal carboxylate and its amide analogues were studied.
Adres publiczny
https://doi.org/10.1039/B107412C
Strona internetowa wydawcy
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