Abstract
Human serum albumin accumulates low molecular weight biomarkers related to cancer. This accumulation can lead to allosteric modification of albumin and change its ability to bind essential fatty acids. Using 16-doxyl-stearic acid spin probe, which is specific for albumin, the serum samples of 98 patients with a variety of cancer types and 86 cancer free individuals were analysed by electron spin resonance (ESR) spectroscopy in order to evaluate cancer-induced modifications that occur to albumin. The ESR spectra showed significant differences between the investigated groups. These differences were most apparent in the intensities and widths of the spectral lines corresponding to the different types of albumin binding sites.
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