Plant flavonol quercetin and isoflavone biochanin A differentially induce protection against oxidative stress and inflammation in ARPE-19 cells

In this work, differential ability of plant flavonol quercetin and plant isoflavone biochanin A to modulate oxidative stress and inhibit inflammation-related responses was investigated using human retinal pigment epithelial cells (RPE) at gene expression level. Quercetin protected cells from oxidative stress-induced cell death, whereas biochanin A had no statistically significant protective effects. Quercetin reduced the expression of cytokines IL-6 and IL-1?? in cells treated with H₂O₂, and expression levels of Nrf2 and HO-1 were increased by quercetin treatment suggesting protective function against oxidative stress. Our data indicate that quercetin may protect cells by inhibiting the production of pro-inflammatory factors such as IL-6, and by inducing the expression of ROS-catalyzing phase II proteins such as HO-1. Therefore, plant extracts rich in flavonol quercetin may be an interesting resource for functional food products and other foods targeted for reduced risks of age-related macular degeneration.     

Acceleration of the thermoxidation of oil by heme iron

Transition metals, including iron, occur naturally at significant concentrations in meat. Iron can be extracted from the food into the oil and potentially decrease the stability of the oil during frying by accelerating thermoxidation. The objective was to examine the thermoxidative stability of partially hydrogenated soybean oil after addition of heme iron. Heme iron (2.7 ppm) was added to the oil, and then oil samples were heated continuously at 160, 180, or 200°C for 72 h. Oil samples were removed for analysis every 12 h. The acid values, color, food oil sensor readings, and TAG polymer content of the heated oil samples were compared with oil samples containing no added iron that were held at the same temperatures. Generally, each oxidative index increased with (i) an increase in temperature, (ii) an increase in heating time, and/or (iii) the addition of iron. Generally, the extent of oxidation was greater for samples heated at 200°C than for oil samples heated at 160 or 180°C. The oil samples heated at 200°C reached the target polymer content of 20% after 27 h of heating. If heme iron accumulates in the oil, it will increase the rate of oxidation and thermal degradation and reduce the frying life of the oil.     

Rational Design of Domain‐Swapping‐Based c‐Type Cytochrome Heterodimers by Using Chimeric Proteins

The design of protein oligomers with multiple active sites has been gaining interest, owing to their potential use for biomaterials, which has encouraged researchers to develop a new design method. Three‐dimensional domain swapping is the unique phenomenon in which protein molecules exchange the same structural region between each other. Herein, to construct oligomeric heme proteins with different active sites by utilizing domain swapping, two c‐type cytochrome‐based chimeric proteins have been constructed and the domains swapped. According to X‐ray crystallographic analysis, the two chimeric proteins formed a domain‐swapped dimer with two His/Met coordinated hemes. By mutating the heme coordination structure of one of the two chimeric proteins, a domainswapped heterodimer with His/Met and His/H₂O coordinated hemes was formed. Binding of an oxygen molecule to the His/H₂O site of the heterodimer was confirmed by resonance Raman spectroscopy, in which the Fe?O₂ stretching band was observed at 580 cm^?1 for the reduced/oxygenated heterodimer (at 554 cm^?1 under an ¹⁸O₂ atmosphere). These results show that domain swapping is a useful method to design multiheme proteins.     

Hemoglobin(βC93A)–Albumin Cluster: Mutation of Cysteine-β93 to Alanine Allows Moderate Reduction of O2 Affinity by Inositol Hexaphosphate

Covalent wrapping of recombinant human hemoglobin (Cys-β93→Ala) variant rHb(βC93A) by human serum albumin (HSA) yielded the rHb(βC93A)-HSA₃ cluster as an artificial O₂ carrier as a red blood cell substitute. Complexation of inositol hexaphosphate to the central rHb(βC93A) core reduced the O₂ affinity moderately, in much the same way as that of naked hemoglobin. This reduction might be attributable to the inert, small Ala-β93 residue, which cannot be reacted with the bulky maleimide crosslinker.