Abstract
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
Similar content being viewed by others
References
Newman DJ, Cragg GM (2007) J Nat Prod 70:461–477
Balunas MJ, Kinghorn AD (2005) Life Sci 78:431–441
Goel A, Kunnumakkara AB, Aggarwal BB (2008) Biochem Pharmacol 75:787–809
Ganesan A (2008) Curr Opin Chem Biol 12:306–317
Maheshwari RK, Singh AK, Gaddipati J, Srimal RC (2006) Life Sci 78:2081–2087
Sharma RA, Gescher AJ, Steward WP (2005) Eur J Cancer 41:1955–1968
Menon VP, Sudheer AR (2007) Springer, New York
Zorofchian Moghadamtousi S, Abdul Kadir H, Hassandarvish P, Tajik H, Abubakar S, Zandi K (2014) BioMed Res Int 2014:1–12
Salem M, Rohani S, Gillies ER (2014) RSC Adv 4:10815–10829
Ono M, Higuchi T, Takeshima M, Chen C, Nakano S (2013) Anticancer Res 33:1861–1866
Senft C, Polacin M, Priester M, Seifert V, Kögel D, Weissenberger J (2010) BMC Cancer 10:491
Liu D, Schwimer J, Liu Z, Woltering EA, Greenway FL (2008) Pharm Biol 46:677–682
Mishra S, Palanivelu K (2008) Ann Indian Acad Neurol 11:13
Accurso F, Pediatr J (2004) Gastroenterol Nutr 39:235
Mythri RB, SrinivasBharath MM (2012) Curr Pharm Des 18:91–99
Wongcharoen W, Phrommintikul A (2009) Int J Cardiol 133:145–151
Chuengsamarn S, Rattanamongkolgul S, Luechapudiporn R, Phisalaphong C, Jirawatnotai S (2012) Diabetes Care 35:2121–2127
Manjunatha H, Srinivasan K (2007) Lipids 42:1133–1142
Aggarwal BB, Harikumar KB (2009) Int J Biochem Cell Biol 41:40–59
Wang YJ, Pan MH, Cheng AL, Lin LI, Ho YS, Hsieh CY, Lin JK (1997) J Pharm Biomed Anal 15:1867–1876
Shen L, Ji HF (2012) Trends Mol Med 18:138–144
Priyadarsini KI (2009) J Photochem Photobiol C 10:81–96
Price LC, Buescher RW (1997) J Food Sci 62:267–269
Canamares MV, Garcia-Ramos JV, Sanchez-Cortes S (2006) Appl Spectrosc 60:1386–1391
Mattia A, Ferrari E, Croci S, Atti G, Rubagotti S, Iori M, Capponi PC, Zerbini A, Saladini M, Versari A (2014) Inorg Chem 53:4922–4933
Vajragupta O, Boonchoong P, Berliner LJ (2004) Free Radical Res 38:303–314
Thompson KH, Böhmerle K, Polishchuk E, Martins C, Toleikis P, Tse J, Orvig C (2004) J Inorg Biochem 98:2063–2070
Mohammadi K, Thompson KH, Patrick BO, Storr T, Martins C, Polishchuk E, Orvig C (2005) J Inorg Biochem 99:2217–2225
Barik A, Mishra B, Kunwar A, Kadam RM, Shen L, Dutta S, Indira Priyadarsini K (2007) Eur J Inorg Chem 42:431–439
Valentini A, Conforti F, Crispini A, De Martino A, Condello R, Stellitano C, Pucci D (2008) J Med Chem 52:484–491
Reddy S, Aggarwal BB (1994) FEBS Lett 341:19–22
Skrzypczak-Jankun E, McCabe NP, Selman SH, Jankun J (2000) Int J Mol Med 6:521–527
Hu GX, Lin H, Lian QQ, Zhou SH, Guo J, Zhou HY, Ge RS (2013) PLoS One 8:e49976
Sui Z, Salto R, Li J, Craik C, Ortiz de Montellano PR (1993) Bioorg Med Chem 1:415–422
Vajragupta P, Boonchoong O, Morris GM, Olson AJ (2005) Bioorg Med Chem Lett 15:3364–3368
Liu M, Yuan M, Luo M, Bu X, Luo HB, Hu X (2010) Biophys Chem 147:28–34
Shen L, Ji HF (2009) Bioorg Med Chem Lett 19:5990–5993
Ngo TT (2010) Anal Lett 43:1572–1587
Veitch NC (2004) Phytochem 65:249–259
Gajhede M, Schuller DJ, Henriksen A, Smith AT, Poulos TL (1997) Nat Struct Mol Biol 4:1032–1038
Wright DG (2012) Chem Biol 19:3–10
Alanis JA (2005) Arch Med Res 36:697–705
Han S, Yang Y (2005) Dyes Pigm 64:157–161
Varaprasad K, Vimala K, Ravindra S, Reddy NN, Reddy GV, Raju KM (2011) J Mater Sci Mater Med 22:1863–1872
Liu CH, Huang HY (2012) Chem Pharm Bull 60:1118–1124
Niamsa N, Sittiwet C (2009) J Pharmacol Toxicol 4:173–177
Lawhavinit OA, Kongkathip N, Kongkathip B (2010) Kasetsart J Nat Sci 44:364–371
Mun SH, Joung DK, Kim YS, Kang OH, Kim SB, Seo YS, Kwon DY (2013) Phytomedicine 20:714–718
Tajbakhsh S, Mohammadi K, Deilami I, Zandi K, Fouladvand M, Ramedani E, Asayesh G (2008) Afr J Biotechnol 7:3832–3835
Trinder P (1969) Ann Clin Biochem 6:24–27
Low PS, Bada JL, Somero GN (1973) Proc Natl Acad Sci 70:430–432
Hassani L, Nourozi R (2014) Appl Biochem Biotechnol 172:3558–3569
Kelly SM, Price NC (2000) Curr Protein Peptide Sci 1:349–384
Mosmann T (1983) J Immunol Methods 65:55–63
Reller LB, Weinstein M, Jorgensen JH, Ferraro MJ (2009) Clin Infect Dis 49:1749–1755
Schomburg D, Salzmann M, Stephan D (1994) Enzyme handbook, vol 7. Springer, Berlin, Heidelberg
Halliwell B, Gutteridge J (1989) Free radicals in biology and medicine, 2nd edn. Oxford University Press, Oxford
Copeland RA (2000) Enzymes: a practical introduction to structure, mechanism, and data analysis. Wiley, New York
Lonhienne T, Gerday C, Feller G (2000) Biochim Biophys Acta (BBA) Protein Struct Mol Enzymol 1543:1–10
Kelly SM, Jess TJ, Price NC (2005) Biochim Biophys Acta (BBA) Proteins Proteomics 1751:119–139
Lakowicz JR (2006) Principles of fluorescence spectroscopy, 3rd edn. Springer, New York
Campbell ID, Dwek RA (1984) Biological spectroscopy. Benjamin Cummings Pub. Co, California
Tsaprailis G, Chan DWS, English AM (1998) Biochemistry 37:2004–2016
Wu BP, Wen Q, Xu H, Yang Z (2014) J Mol Catal B Enzym 101:101–107
Bobone S, van de Weert M, Stella L (2014) J Mol Struct 1077:68–76
Mohammadi F, Bordbar A, Divsalar A, Mohammadi K, Saboury AA (2009) Protein J 28:117–123
Mohammadi F, Bordbar A, Divsalar A, Mohammadi K, Saboury AA (2009) Protein J 28:189–196
Mohammadi F, Bordbar A, Mohammadi K, Divsalar A, Saboury AA (2010) Can J Chem 88:155–163
Acknowledgments
The authors express their sincere thanks to the Research Council of Institute for Advanced Studies in Basic Sciences for its financial support for this work.
Author information
Authors and Affiliations
Corresponding author
Electronic supplementary material
Below is the link to the electronic supplementary material.
Rights and permissions
About this article
Cite this article
Jahangoshaei, P., Hassani, L., Mohammadi, F. et al. 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. J Biol Inorg Chem 20, 1135–1146 (2015). https://doi.org/10.1007/s00775-015-1295-x
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00775-015-1295-x