N,N-Diallyl methionine ethyl ester hydrochloride 5 underwent alternating copolymerization with SO_2 via the Butler cyclopolymerization protocol in dimethyl sulfoxide(DMSO) to give water-soluble cycloterpolymer 6 with...N,N-Diallyl methionine ethyl ester hydrochloride 5 underwent alternating copolymerization with SO_2 via the Butler cyclopolymerization protocol in dimethyl sulfoxide(DMSO) to give water-soluble cycloterpolymer 6 with a ～1:1 molar ratio of sulfide and sulfoxide groups as a result of oxygen transfer from DMSO. Half of the sulfide groups in 6, upon oxidation with H_2O_2, afforded polymer sulfoxide 7 and polymer sulfone 8. The solution properties of these polymers were determined via a viscometric technique. The thermal stability of these polymers was determined by thermogravimetric analysis. The inhibition efficiency obtained from gravimetric mass loss, potentiodynamic polarization, and electrochemical impedance spectroscopy techniques agreed well with each other. The corrosion efficiencies increase with increasing concentration of the polymers. At a polymer concentration of 175 mM, the maximum inhibition efficiency of copolymer compounds 6–8 was determined to be 92%, 97%, and 95%, respectively. The synthesized polymer compounds acted as mixed-type inhibitors. Polymer compound 7 adsorbed onto the metal surface via chemisorption and physisorption and obeyed Langmuir, Temkin, and Freundlich adsorption isotherms. Analyses by X-ray photoelectron spectroscopy and scanning electron microscopy–energy-dispersive X-ray spectroscopy indicated that the adsorbed polymers formed a thin film on the metal surface and prevented further corrosive attack.展开更多
以蛋氨酸和长链脂肪酸为原料,合成了4种不同碳链长度的含亚砜基蛋氨酸型表面活性剂（CnMSO）。通过FTIR、1HNMR和ESI-MS表征了产物的结构,并对该系列表面活性剂的表面张力、临界胶束浓度（CMC）、乳化性能、发泡性能、硬水稳定性和抑菌...以蛋氨酸和长链脂肪酸为原料,合成了4种不同碳链长度的含亚砜基蛋氨酸型表面活性剂（CnMSO）。通过FTIR、1HNMR和ESI-MS表征了产物的结构,并对该系列表面活性剂的表面张力、临界胶束浓度（CMC）、乳化性能、发泡性能、硬水稳定性和抑菌性能进行了测定。结果表明,该系列的表面活性剂的最低表面张力（γCMC）为21-24 m N/m,临界胶束浓度为0.15-1.5 mmol/L,在硬水中的平均稳定性均在3级以上,具有良好的泡沫性能和乳化性能。另外,产物对大肠杆菌、金黄色葡萄球菌和白色念珠菌的生长抑制作用明显,抑菌性优于N-月桂酰谷氨酸（C12G）。展开更多
Methionine oxidation to methionine sulfoxide （MetSO） is reversed by two types of methionine sulfoxide reducrases （MSRs）, A and B, specific to the S- and R-diastereomers of MetSO, respectively. MSR genes are found ...Methionine oxidation to methionine sulfoxide （MetSO） is reversed by two types of methionine sulfoxide reducrases （MSRs）, A and B, specific to the S- and R-diastereomers of MetSO, respectively. MSR genes are found in most organisms from bacteria to human. In the current review, we first compare the organization of the MSR gene families in photosynthetic organisms from cyanobacteria to higher plants. The analysis reveals that MSRs constitute complex families in higher plants, bryophytes, and algae compared to cyanobacteria and all non-photosynthetic organisms. We also perform a classification, based on gene number and structure, position of redox-active cysteines and predicted sub-cellular localization. The various catalytic mechanisms and potential physiological electron donors involved in the regeneration of MSR activity are then de- scribed. Data available from higher plants reveal that MSRs fulfill an essential physiological function during environmental constraints through a role in protein repair and in protection against oxidative damage. Taking into consideration the ex- pression patterns of MSR genes in plants and the known roles of these genes in non-photosynthetic cells, other functions of MSRs are discussed during specific developmental stages and ageing in photosynthetic organisms.展开更多
Methionine is a highly susceptible amino acid that can be oxidized to S and R diastereomeric forms of methionine sulfoxide by many of the reactive oxygen species generated in biological systems. Methionine sulfoxide r...Methionine is a highly susceptible amino acid that can be oxidized to S and R diastereomeric forms of methionine sulfoxide by many of the reactive oxygen species generated in biological systems. Methionine sulfoxide reductases (Msrs) are thioredoxin-linked enzymes involved in the enzymatic conversion of methionine sulfoxide to methionine. Although MsrA and MsrB have the same function of methionine reduction, they differ in substrate specifi city, active site composition, subcellular localization, and evolution. MsrA has been localized in different ocular regions and is abundantly expressed in the retina and in retinal pigment epithelial (RPE) cells. MsrA protects cells from oxidative stress. Overexpression of MsrA increases resistance to cell death, while silencing or knocking down MsrA decreases cell survival; events that are mediated by mitochondria. MsrA participates in protein-protein interaction with several other cellular proteins. The interaction of MsrAwith α-crystallins is of utmost importance given the known functions of the latter in protein folding, neuroprotection, and cell survival. Oxidation of methionine residues in α-crystallins results in loss of chaperone function and possibly its antiapoptotic properties. Recent work from our laboratory has shown that MsrA is co-localized with αA and αB crystallins in the retinal samples of patients with age-related macular degen- eration. We have also found that chemically induced hypoxia regulates the expression of MsrA and MsrB2 in human RPE cells. Thus, MsrA is a critical enzyme that participates in cell and tissue protection, and its interaction with other proteins/growth factors may provide a target for therapeutic strategies to prevent degenerative diseases.展开更多
基金financial assistance of the Deanship of Scientific Research, KFUPM, Saudi Arabia through Internal project # IN131047
文摘N,N-Diallyl methionine ethyl ester hydrochloride 5 underwent alternating copolymerization with SO_2 via the Butler cyclopolymerization protocol in dimethyl sulfoxide(DMSO) to give water-soluble cycloterpolymer 6 with a ～1:1 molar ratio of sulfide and sulfoxide groups as a result of oxygen transfer from DMSO. Half of the sulfide groups in 6, upon oxidation with H_2O_2, afforded polymer sulfoxide 7 and polymer sulfone 8. The solution properties of these polymers were determined via a viscometric technique. The thermal stability of these polymers was determined by thermogravimetric analysis. The inhibition efficiency obtained from gravimetric mass loss, potentiodynamic polarization, and electrochemical impedance spectroscopy techniques agreed well with each other. The corrosion efficiencies increase with increasing concentration of the polymers. At a polymer concentration of 175 mM, the maximum inhibition efficiency of copolymer compounds 6–8 was determined to be 92%, 97%, and 95%, respectively. The synthesized polymer compounds acted as mixed-type inhibitors. Polymer compound 7 adsorbed onto the metal surface via chemisorption and physisorption and obeyed Langmuir, Temkin, and Freundlich adsorption isotherms. Analyses by X-ray photoelectron spectroscopy and scanning electron microscopy–energy-dispersive X-ray spectroscopy indicated that the adsorbed polymers formed a thin film on the metal surface and prevented further corrosive attack.
文摘以蛋氨酸和长链脂肪酸为原料,合成了4种不同碳链长度的含亚砜基蛋氨酸型表面活性剂（CnMSO）。通过FTIR、1HNMR和ESI-MS表征了产物的结构,并对该系列表面活性剂的表面张力、临界胶束浓度（CMC）、乳化性能、发泡性能、硬水稳定性和抑菌性能进行了测定。结果表明,该系列的表面活性剂的最低表面张力（γCMC）为21-24 m N/m,临界胶束浓度为0.15-1.5 mmol/L,在硬水中的平均稳定性均在3级以上,具有良好的泡沫性能和乳化性能。另外,产物对大肠杆菌、金黄色葡萄球菌和白色念珠菌的生长抑制作用明显,抑菌性优于N-月桂酰谷氨酸（C12G）。
文摘Methionine oxidation to methionine sulfoxide （MetSO） is reversed by two types of methionine sulfoxide reducrases （MSRs）, A and B, specific to the S- and R-diastereomers of MetSO, respectively. MSR genes are found in most organisms from bacteria to human. In the current review, we first compare the organization of the MSR gene families in photosynthetic organisms from cyanobacteria to higher plants. The analysis reveals that MSRs constitute complex families in higher plants, bryophytes, and algae compared to cyanobacteria and all non-photosynthetic organisms. We also perform a classification, based on gene number and structure, position of redox-active cysteines and predicted sub-cellular localization. The various catalytic mechanisms and potential physiological electron donors involved in the regeneration of MSR activity are then de- scribed. Data available from higher plants reveal that MSRs fulfill an essential physiological function during environmental constraints through a role in protein repair and in protection against oxidative damage. Taking into consideration the ex- pression patterns of MSR genes in plants and the known roles of these genes in non-photosynthetic cells, other functions of MSRs are discussed during specific developmental stages and ageing in photosynthetic organisms.
基金Supported by Grants from NIH (EY01545, EY03040)The Arnold and Mabel Beckman Foundation (to Hinton DR)a grant to the Department of Ophthalmology by Research to Prevent Blindness
文摘Methionine is a highly susceptible amino acid that can be oxidized to S and R diastereomeric forms of methionine sulfoxide by many of the reactive oxygen species generated in biological systems. Methionine sulfoxide reductases (Msrs) are thioredoxin-linked enzymes involved in the enzymatic conversion of methionine sulfoxide to methionine. Although MsrA and MsrB have the same function of methionine reduction, they differ in substrate specifi city, active site composition, subcellular localization, and evolution. MsrA has been localized in different ocular regions and is abundantly expressed in the retina and in retinal pigment epithelial (RPE) cells. MsrA protects cells from oxidative stress. Overexpression of MsrA increases resistance to cell death, while silencing or knocking down MsrA decreases cell survival; events that are mediated by mitochondria. MsrA participates in protein-protein interaction with several other cellular proteins. The interaction of MsrAwith α-crystallins is of utmost importance given the known functions of the latter in protein folding, neuroprotection, and cell survival. Oxidation of methionine residues in α-crystallins results in loss of chaperone function and possibly its antiapoptotic properties. Recent work from our laboratory has shown that MsrA is co-localized with αA and αB crystallins in the retinal samples of patients with age-related macular degen- eration. We have also found that chemically induced hypoxia regulates the expression of MsrA and MsrB2 in human RPE cells. Thus, MsrA is a critical enzyme that participates in cell and tissue protection, and its interaction with other proteins/growth factors may provide a target for therapeutic strategies to prevent degenerative diseases.
