Reading of protein surfaces in the native state at micromolar concentrations by a chirogenetic porphyrin probe.
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).
Dipartimento di Scienze Chimiche, Università di Catania, Viale A. Doria, 6, 95125 Catania, Italy. gmineo@unict.it
Placido
P
Mineo
Norberto
N
Micali
Valentina
V
Villari
Maria Grazia
MG
Donato
Emilio
E
Scamporrino
D000596:Amino Acids / Q000737:chemistry*; D002942:Circular Dichroism; D003035:Cobalt / Q000737:chemistry*; D008665:Metalloporphyrins / Q000737:chemistry*; D015394:Molecular Structure; D011166:Porphyrins / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
D000596:Amino Acids; D008665:Metalloporphyrins; D011166:Porphyrins; D011506:Proteins; D003035:Cobalt