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Abstract
The combination of zinc dyshomoeostasis and oxidative damage has been linked to a number of human disease pathologies. A common pathway of oxidative damage centers on tyrosine with the generation of 3,4-dihydroxyphenylalanine (l-dopa). Once formed this catecholic moiety can be involved in metal binding. Herein, an l-dopa residue is incorporated into a peptide designed to adopt a β-hairpin configuration. Variation of the cross strand partner to l-dopa introduces an aromatic pair to enhance structure. Mass spectrometry indicates successful zinc binding, consistent with a 1:1 peptide:zinc complex. NMR and spectrophotometric investigations reveal the l-dopa as the binding locus with association energies ranging between 4.3 and 5.2kcalmol−1.
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