Investigating the effect of gallium curcumin and gallium diacetylcurcumin complexes on the structure, function and oxidative stability of the peroxidase enzyme and their anticancer and antibacterial activities
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| 024 | 7 | 0 | |a 10.1007/s00775-015-1295-x |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-015-1295-x | ||
| 245 | 0 | 0 | |a Investigating the effect of gallium curcumin and gallium diacetylcurcumin complexes on the structure, function and oxidative stability of the peroxidase enzyme and their anticancer and antibacterial activities |h [Elektronische Daten] |c [Parisa Jahangoshaei, Leila Hassani, Fakhrossadat Mohammadi, Akram Hamidi, Khosro Mohammadi] |
| 520 | 3 | |a Curcumin has a wide spectrum of biological and pharmacological activities including anti-inflammatory, antioxidant, antiproliferative, antimicrobial and anticancer activities. Complexation of curcumin with metals has gained attention in recent years for improvement of its stability. In this study, the effect of gallium curcumin and gallium diacetylcurcumin on the structure, function and oxidative stability of horseradish peroxidase (HRP) enzyme were evaluated by spectroscopic techniques. In addition to the enzymatic investigation, the cytotoxic effect of the complexes was assessed on bladder, MCF-7 breast cancer and LNCaP prostate carcinoma cell lines by MTT assay. Furthermore, antibacterial activity of the complexes against S. aureus and E. coli was explored by dilution test method. The results showed that the complexes improve activity of HRP and also increase its tolerance against the oxidative condition. After addition of the complexes, affinity of HRP for hydrogen peroxide substrate decreases, while the affinity increases for phenol substrate. Circular dichroism, intrinsic and synchronous fluorescence spectra showed that the enzyme structure around the catalytic heme group becomes less compact and also the distance between the heme group and tryptophan residues increases due to binding of the complexes to HRP. On the whole, it can be concluded that the change in the enzyme structure upon binding to the gallium curcumin and gallium diacetylcurcumin complexes results in an increase in the antioxidant efficiency and activity of the peroxidise enzyme. The result of anticancer and antibacterial activities suggested that the complexes exhibit the potential for cancer treatment, but they have no significant antibacterial activity. Graphical Abstract: | |
| 540 | |a SBIC, 2015 | ||
| 690 | 7 | |a Gallium curcumin |2 nationallicence | |
| 690 | 7 | |a Horseradish peroxidase |2 nationallicence | |
| 690 | 7 | |a Function |2 nationallicence | |
| 690 | 7 | |a Structure |2 nationallicence | |
| 690 | 7 | |a Antioxidant |2 nationallicence | |
| 700 | 1 | |a Jahangoshaei |D Parisa |u Department of Biological Sciences, Institute for Advanced Studies in Basic Sciences (IASBS), 45195-1159, Zanjan, Iran |4 aut | |
| 700 | 1 | |a Hassani |D Leila |u Department of Biological Sciences, Institute for Advanced Studies in Basic Sciences (IASBS), 45195-1159, Zanjan, Iran |4 aut | |
| 700 | 1 | |a Mohammadi |D Fakhrossadat |u Department of Chemistry, Institute for Advanced Studies in Basic Sciences (IASBS), 45195-1159, Zanjan, Iran |4 aut | |
| 700 | 1 | |a Hamidi |D Akram |u Department of Biological Sciences, Institute for Advanced Studies in Basic Sciences (IASBS), 45195-1159, Zanjan, Iran |4 aut | |
| 700 | 1 | |a Mohammadi |D Khosro |u Chemistry Department, Faculty of Sciences, Persian Gulf University, 75169, Bushehr, Iran |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/7(2015-10-01), 1135-1146 |x 0949-8257 |q 20:7<1135 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-015-1295-x |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-015-1295-x |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Jahangoshaei |D Parisa |u Department of Biological Sciences, Institute for Advanced Studies in Basic Sciences (IASBS), 45195-1159, Zanjan, Iran |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Hassani |D Leila |u Department of Biological Sciences, Institute for Advanced Studies in Basic Sciences (IASBS), 45195-1159, Zanjan, Iran |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Mohammadi |D Fakhrossadat |u Department of Chemistry, Institute for Advanced Studies in Basic Sciences (IASBS), 45195-1159, Zanjan, Iran |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Hamidi |D Akram |u Department of Biological Sciences, Institute for Advanced Studies in Basic Sciences (IASBS), 45195-1159, Zanjan, Iran |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Mohammadi |D Khosro |u Chemistry Department, Faculty of Sciences, Persian Gulf University, 75169, Bushehr, Iran |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/7(2015-10-01), 1135-1146 |x 0949-8257 |q 20:7<1135 |1 2015 |2 20 |o 775 | ||