Publication | Closed Access
Absorption spectroscopy and binding constants for first-row transition metal complexes of a DOPA-containing peptide
102
Citations
33
References
2005
Year
EngineeringPeptide EngineeringBinding ConstantsAbsorption SpectroscopyChemistryChemical BiologySpectra-structure CorrelationDopa-containing PeptideMolecular RecognitionAdopatp PeptideMolecular SpectroscopyBiophysicsInorganic ChemistryBiochemistryDopa-containing MoleculesPhysical ChemistryNon-peptide LigandNatural SciencesPeptide LibraryPeptide SynthesisMolecular Complex
A diverse array of biological systems incorporate 3,4-dihydroxyphenlyalanine (DOPA) into proteins and small molecules for cross-linking and material generation. Marine worm eggshells, sea squirt wound plugs, and marine mussel adhesives may all be formed by combining DOPA-containing molecules with high levels of metals. In order to provide model systems for characterizing these biomaterials, we carried out a study on metal binding to a DOPA-containing peptide. Ultraviolet-visible absorption spectra are presented for the AdopaTP peptide binding to Fe3+, V3+, VO2+, Mn3+, Ti4+, Cu2+, Co2+, and Ni2+ in mono, bis, and where applicable, tris coordination modes. Association constants were determined for selected metal ions binding to the peptide. In general, the spectroscopic and binding properties of this DOPA-containing peptide were found to be similar to those of catechol.
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