Impact of the peptide sequence on the coordination abilities of albumin-like tripeptides towards Cu2+, Ni2+ and Zn2+ ions. Potential albumin-like peptide chelatorsElectronic supplementary information (ESI) available: Tables S1–S3 and Fig. S1–S4 described in the text. See http://www.rsc.org/suppdata/nj/b1/b107412c/

Abstract

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.