BIOL 171 |
| Serum proteins are potential carriers of antineoplastic agents due to their accumulation in tumour tissue. Human Serum Albumin (HSA) is the most abundant blood plasma protein, plays a key role in the transport of fatty acids, metabolites and drugs. In the present study, we attempt to identify the specific binding site for chlorin p6 in HSA. The binding constants and the number of binding sites have been ascertained from the quenching of the fluorescence of the single Tryptophanyl residue of HSA by the photosensitizer. A significant energy transfer from Trp-214 to chlorin p6 indicates that it most likely to have been bound to the vicinity of Sudlow's site I. In order to further verify this result, the competitive binding of the photosensitizer with warfarin has been monitored by time resolved fluorescence spectroscopy, as this site is the primary binding site for warfarin. A global analysis of the data reveals that chlorin p6 displaces warfarin from its conjugates with HSA, which confirms that it indeed binds to Sudlow's site I. |
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Frontiers in Chemical Biology
5:00 PM-7:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Biological Chemistry |