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Updated: Jun 25, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Short-chain oligopeptides with copper(II) binding properties: The impact of specific structural modifications on the
Agnieszka Matera-Witkiewicz1, Justyna Brasuń, Jolanta Swiatek-Kozłowska
1Department of Inorganic Chemistry, Medical University of Wrocław, Szewska, Poland.
Abstract:
A series of linear tetrapeptides containing two histidyl residues in position 2 and 4, namely DHGH, DHGdH, KHGH, KHGdH, Ac-DHGH-NH(2), Ac-DHGdH-NH(2), Ac-KHGH-NH(2), and Ac-KHGdH-NH(2), were synthesized and characterised. Their copper(II) binding properties were investigated in depth through a variety of physicochemical methods. Potentiometric titrations were first carried out to establish the stoichiometry and the stability of the resulting copper(II)-peptide complexes. The copper(II) chromophores that are formed in the various cases in dependence of pH were subsequently characterised by extensive spectroscopic analysis (UV-Vis, EPR, CD) in strict correlation with potentiometric data. The effects of the nature of the first amino acid (Lys versus Asp) and of N-terminal amino group protection on copper(II) binding were specifically addressed. On turn, the careful comparison of the copper(II) coordination abilities of the linear peptides with those of their cyclic analogs provided insight into the effects of cyclization on the overall metal binding properties.
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