Thermodynamic and spectroscopic studies have shown that the insertion of alpha-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.
Mlynarz, P., Valensin, D., Kociolek, K., Zabrocki, J., Kozlowski, J., Olejnik, H. (2002). Impact of the peptide sequence on the coordination abilities of albumin-like tripeptides towards Cu2+, Ni2+, Zn2+ ions. Potential albumin-like peptides chelators. NEW JOURNAL OF CHEMISTRY, 26(2), 264-268 [10.1039/b107412c].
Impact of the peptide sequence on the coordination abilities of albumin-like tripeptides towards Cu2+, Ni2+, Zn2+ ions. Potential albumin-like peptides chelators
Valensin, Daniela;
2002-01-01
Abstract
Thermodynamic and spectroscopic studies have shown that the insertion of alpha-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.
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https://hdl.handle.net/11365/12120
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