سال انتشار: ۱۳۸۷
محل انتشار: دومین کنگره بین المللی علوم و فناوری نانو
تعداد صفحات: ۲
S.V Shetab Boushehri – Department of Medical Nanotechnology, School of Advance Technology in Medical Sciences, Tehran University
b Salmanian –
a Omidvari –
s Esmaili –
Up to recently, a not-too-long list of the mitochondrial porphyrin-binding proteins (PBP) was strictly limited to well known heme-containing molecules like cytochromes or peroxidases . In external membrane of mammalian mitochondria, however, some minor group of proteins with a marked capability for selective binding of porphyrin K and its derivatives but with no direct link to either heme or any other porphyrin in situ has been found lately . Both functional role and structural peculiarities of these specific membrane proteins remains obscure which requires a reliable method to isolate / purify these unique compounds for their further study.The porphyrin – engaging ligands look suitable for affinity chromatography of PBP and related compounds. It is not easy, nonetheless, to reach a perfect protein – ligand coupling as long as the whole stationary phase molecular architecture does not allow to make it stoichiometrically (nanotopologically) correct. Due to this, a number of technical problems are found to be the hard obstacles on a way to the PBP affinity chromatography developments .To solve these problems, we have proposed an affinity chromatography technique based on application of a new stationary phase possessing the porphyrin domain as a ligand attached to the complex epoxy[cyclohecyl]C60-fullerene spacer immobilized firmly on an agarose gel matrix. In the best of our knowledge, this is the first report ever on the fullerene nanostructure use to optimize a protein-porphyrin recognition in affinity coupling.