Ovarian cancer is one of the primary causes of death for women all through the Western world. Baicalin and baicalein are naturally occurring flavonoids that are found in the roots and leaves of some Chinese medicinal plants and are thought to have antioxidant activity and possible anti-angiogenic, anti-cancer, anxiolytic, anti-inflammatory and neuroprotective activities. Two kinds of ovarian cancer (OVCAR-3 and CP-70) cell lines and a normal ovarian cell line (IOSE-364) were selected to be investigated in the inhibitory effect of baicalin and baicalein on cancer cells. Largely, baicalin and baicalein inhibited ovarian cancer cell viability in both ovarian cancer cell lines with LD₅₀ values in the range of 45–55 µM for baicalin and 25–40 µM for baicalein. On the other hand, both compounds had fewer inhibitory effects on normal ovarian cells viability with LD₅₀ values of 177 µM for baicalin and 68 µM for baicalein. Baicalin decreased expression of VEGF (20 µM), cMyc (80 µM), and NFkB (20 µM); baicalein decreased expression of VEGF (10 µM), HIF-1α (20 µM), cMyc (20 µM), and NFkB (40 µM). Therefore baicalein is more effective in inhibiting cancer cell viability and expression of VEGF, HIF-1α, cMyc, and NFκB in both ovarian cancer cell lines. It seems that baicalein inhibited cancer cell viability through the inhibition of cancer promoting genes expression including VEGF, HIF-1α, cMyc, and NFκB. Overall, this study showed that baicalein and baicalin significantly inhibited the viability of ovarian cancer cells, while generally exerting less of an effect on normal cells. They have potential for chemoprevention and treatment of ovarian cancers.

The effect of different cooking methods on protein and lipid oxidation of farmed sturgeon (Acipenser gueldenstaedtii) was investigated. In this study, the fish fillets were cooked using five different methods (boiling, steaming, microwaving, roasting and deep-frying), to an internal temperature of approximately 85 °C. General indexes for protein oxidation (carbonyls, free thiols and Schiff bases) and lipid oxidation were evaluated by spectrophotometric and fluorimetric methods. Side-chain modifications of amino acid residues were pinpointed by gel- and MS-based proteomic technology. The results are as follows: (1) cooking, especially roasting and frying, significantly increased the levels of carbonyls and Schiff bases and decreased the amounts of free thiols. (2) Oxidation of aromatic amino acids and extensive oxidation of lysine to carbonyl-containing compounds were characterized in all the cooked samples. (3) Indirect protein oxidation caused by interacting with lipid-derived aldehydes like malondialdehyde (MDA) and 4-hydroxynonenal (HNE) was also observed and much more pronounced in roasted and fried samples, giving a footprint of lipid–protein interaction during cooking. In summary, cooking treatment can induce protein oxidation in sturgeon fillets with a variety of modifications occurring at the protein primary structure. Molecular mapping of protein oxidation is conducive to understand the mechanism of cooking-induced protein oxidation and allows better control of the nutritional properties of protein-based products.