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

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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. The 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.
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