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Reading of Protein Surfaces in the Native State at Micromolar Concentrations by a Chirogenetic Porphyrin Probe
Author(s) -
Mineo Placido,
Micali Norberto,
Villari Valentina,
Donato Maria Grazia,
Scamporrino Emilio
Publication year - 2012
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201200784
Subject(s) - porphyrin , circular dichroism , chemistry , aqueous solution , globular protein , supramolecular chemistry , amino acid , native state , fluorescence , cobalt , protein structure , crystallography , photochemistry , biochemistry , organic chemistry , crystal structure , physics , quantum mechanics
The recognition of some globular proteins was carried out in aqueous solution, at micromolar concentrations, by using an uncharged symmetrical cobalt–porphyrin (Co–P). By means of UV/Vis, induced circular dichroism, and fluorescence spectroscopy techniques, it was ascertained that the interactions between specific amino acid residues and Co–P occurred on the protein surface. In particular, spectroscopic evidence showed the formation of supramolecular complexes without disruption of the native structure of the proteins and, furthermore, that signal changes were characteristic of each Co–P/protein system, so that they could be used as a highly sensitive analytical tool for protein recognition. The relative association constants were proportional to the protein molecular masses (and then to the number of amino acid residues).