Preparation and antioxidant activity of albumin binding Salen Schiff-base metal complexes

Preparation and antioxidant activity of albumin binding Salen Schiff-base metal complexes
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DOI:
10.1007/s11434-013-5787-1
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发表时间:
2013-04
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通讯作者:
Gang Li;HuiFang Zhang;Rongmin Wang;Yufeng He;Y. Xiong
Gang Li;HuiFang Zhang;Rongmin Wang;Yufeng He;Y. Xiong
中科院分区:
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文献类型:
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作者:
Gang Li;HuiFang Zhang;Rongmin Wang;Yufeng He;Y. Xiong

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采用偶联法合成了一种新型生物高分子抗氧化剂(BSA/HOSalenM,M=Co,Mn,Zn),提高了牛血清白蛋白(BSA)的抗氧化活性。通过红外光谱、紫外-可见光谱、荧光光谱、圆二色谱和非变性聚丙烯酰胺凝胶电泳对偶联物进行了表征。BSA被用作生物聚合物支架,并且不溶性Salen Schiff碱金属络合物HOSalenM与BSA的氨基酸残基进行轴向配位。当HOSalenCo的结合率小于10时,BSA的结构不变。HOSalenCo具有良好的清除羟自由基(·OH)活性,BSA/HOSalenCo(10)(BSA:HOSalenCo=1:10)的EC_(50)比BSA提高了两个数量级,而BSA/HOSalenMn的活性较弱,BSA/HOSalenZn没有清除羟自由基的活性。
A kind of novel biopolymer antioxidant (BSA/HOSalenM, M=Co, Mn, Zn) is prepared with conjugation, which increases the antioxidant activity of the bovine serum albumin (BSA). The conjugations have been characterized by IR spectra, UV-Vis spectra, Fluorescence spectra, Circular dichroism (CD) spectra and Native-PAGE. The BSA is used as a biopolymer scaffold, and the insoluble Salen Schiff-base metal complexes HOSalenM make axial coordination with the amino acid residues of the BSA. The structure of the BSA is unchanged when the binding rate of HOSalenCo is less than 10. The HOSalenCo conjugations show an excellent hydroxyl radical (·OH) scavenging activity, and the activity (EC50) of BSA/HOSalenCo(10) (BSA:HOSalenCo=1:10) is improved by two orders of magnitude compared with the BSA, while the activity of the BSA/HOSalenMn is weak and the BSA/HOSalenZn shows no scavenging activity.