پیوندهای مفید
اخبار و اعلانات
آمار
| تعداد نشریات | 25 |
| تعداد شماره‌ها | 941 |
| تعداد مقالات | 7,773 |
| تعداد مشاهده مقاله | 12,854,090 |
| تعداد دریافت فایل اصل مقاله | 9,152,475 |
بررسی اثر نانوذره اکسید مس بر فعالیت و ساختار آنزیم پراکسیداز لیپیدیوم درابا (LDP) | ||
| زیست شناسی کاربردی | ||
| مقاله 6، دوره 36، شماره 1 - شماره پیاپی 75، خرداد 1402، صفحه 135-158 اصل مقاله (1.45 M) | ||
| نوع مقاله: مقاله پژوهشی | ||
| شناسه دیجیتال (DOI): 10.22051/jab.2023.41224.1500 | ||
| نویسندگان | ||
| علی ریاحی مدوار* 1؛ فرشید برزگری دهج2؛ رضا میرزایی2؛ فهیمه بهرام نژاد3 | ||
| 1دانشیار ،گروه زیست شناسی سلولی-مولکولی، دانشکده علوم پایه، دانشگاه کوثر بجنورد، بجنورد، | ||
| 2دانش‌آموخته کارشناسی ارشد، گروه بیوتکنولوژی، پژوهشگاه علوم و تکنولوژی پیشرفته و علوم محیطی، دانشگاه تحصیلات تکمیلی صنعتی و فناوری پیشرفته، کرمان، ایران. | ||
| 3استادیار، دانشگاه علوم پزشکی جیرفت، جیرفت، ایران. | ||
| چکیده | ||
| مقدمه: ورود نانوذرات به بدن موجودات زنده می‌تواند بر روی ماکرومولکول‌های زیستی اثر گذاشته و حیات آنها را تحت تاثیر قرار دهد. در این مطالعه، تغییرات فعالیت و ساختار آنزیم نوترکیبLDP در حضور نانوذره اکسید‌مس (nCuO) مورد آنالیز قرار گرفت. روش‌ها: فعالیت آنزیم در حضور غلظت‌های مختلف nCuO اندازه‌گیری شد. از مطالعات فلورسانس ذاتی در حضور غلظت‌های مختلف نانوذره و دماهای مختلف جهت بررسی تغییرات ساختاری و تعیین پارامترهای ترمودینامیکی کمپلکس آنزیم-نانوذره استفاده شد. نتایج و بحث: نتایج نشان داد که فعالیت آنزیم در حضور nCuO افزایش می‌یابد. شدت فلورسانس ذاتی در حضور نانوذره در روندی وابسته به غلظت کاهش یافت. آنالیزهای ترمودینامیکی نشان دهنده مثبت بودن آنتالپی و آنتروپی و منفی بودن تغییرات انرژی آزاد واکنش می‌باشند. بر اساس نتایج، تغییر فعالیت آنزیم، حاصل تغییرات ساختاری آنزیم در میانکنش با نانوذره است که این فرایند با استفاده از میانکنش‌های هیدروفوب و بصورت خودبخودی پیش می‌رود. | ||
| کلیدواژه‌ها | ||
| پارامترهای ترمودینامیکی؛ فلورسانس؛ میانکنش‌های هیدروفوب | ||
| عنوان مقاله [English] | ||
| Investigation of the CuO nanoparticles effect on activity and structure of Lepidium draba peroxidase enzyme | ||
| نویسندگان [English] | ||
| Ali Riahi-Madvar1؛ Farshid Barzegary-Dehaj2؛ , Reza Mirzaee2؛ fahiemeh bahramnejad3 | ||
| 1Associate Professor,Department of Molecular and Cell Biology, Faculty of Basic Sciences, Kosar University of Bojnord, Bojnord, Iran | ||
| 2Master's student, Department of Biotechnology, Research Institute of Advanced Science and Technology and Environmental Sciences, Post Graduate University of Industrial and Advanced Technology, Kerman, Iran. | ||
| 3Assistant Professor, Jiroft University of Medical Sciences, Jiroft, Iran. | ||
| چکیده [English] | ||
| Introduction: Entrance nanoparticles into the environment provides possibility of their entry into living organisms body. Their entry into the body can affect biological macromolecules and affect their life. Here, to investigate effect of copper oxide nanoparticle (nCuO) on recombinant Lepidium draba peroxidase, changes in enzyme activity and structure were analyzed in the presence of nCuO. Methods: Enzyme activity was measured in the presence of different concentrations of nCuO and repeated three times. Results were statistically analyzed using SPSS software at a significance level of 5%. Intrinsic fluorescence studies in the presence of nanoparticles were utilized to investigate structural changes of the enzyme. These studies were done at different temperatures to determine thermodynamic parameters such as the type of forces involved in the nanoparticle-enzyme interaction. Results and discussion: Enzyme activity in the presence of nCuO significantly increased at the level of 5%. The most enzyme activity were attributed to the concentration ranges of 80-180 nM nanoparticles, which it increased more than 46% compared to the control. Intrinsic fluorescence intensity decreased in the manner nanoparticles concentrations increased in media. Decrease intrinsic fluorescence emission indicates changes in the enzyme structure in presence of nanoparticle. Thermodynamic parameters including entropy (∆S°) and enthalpy (∆H°) related to the interaction of enzyme with nanoparticle were calculated as 0.108 and 3.81 respectively. The positive sign of these parameters indicates the important role of hydrophobic interactions in this process. On the other hand, negativity of free energy (∆G°) changes indicates that this process is exergonic and proceeds spontaneously. | ||
| کلیدواژه‌ها [English] | ||
| Fluorescence, Hydrophobic interactions, Thermodynamic parameters | ||
|
سایر فایل های مرتبط با مقاله
|
||
| مراجع | ||
|
Ball, P. (2002). Natural strategies for the molecular engineer. Nanotechnology13: 15-28. Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical biochemistry 72(1-2): 248-254. Brandes, N., Welzel, P.B., Werner, C. and Kroh, L.W. (2006) Adsorption-induced conformational changes of proteins onto ceramic particles: differential scanning calorimetry and FTIR analysis. J Colloid Interface Sci 299(1): 56-69. Brunner, T.J., Wick, P., Manser, P., Spohn, P., Grass, R.N., Limbach, L.K., Bruinink, A. and Stark, W.J. (2006). In vitro cytotoxicity of oxide nanoparticles: comparison to asbestos, silica, and the effect ofparticle solubility. Environ Sci Technol 40(14): 4374-4378. Carter, D.C. and Ho, J.X. (1994). Structure of serum albumin. Adv Protein Chem 45: 153−203. Chang, Y.N., Zhang, M., Xia, L., Zhang, J. and Xing, G. (2012). The toxic effects and mechanisms of CuO and ZnO nanoparticles. Materials 5(12): 2850-2871. Chen, L., Wu, M., Lin, X. and Xi, Z. (2011). Study on the interaction between human serum albumin and a novel bioactive acridine derivative using optical spectroscopy. Luminescence 26: 172-177. Dai, P., Mook, H.A., Aeppli, G., Hayden, S.M. and Doğan. F. (2000). Resonance as a measure of pairing correlations in the high-T c superconductor YBa 2 Cu 3 O 6.6. Nature 406(6799): 965. Fattahian, Y., Riahi-Madvar, A., Mirzaee, R., Torkzadeh-Mahani, M. and Asadikaram, G. (2017a). Heterologous Expression, Purification and Characterization of a Peroxidase Isolated from Lepidium draba. The protein journal 36(6): 461-71. Fattahian, Y., Riahi-Madvar, A., Mirzaee, R., Torkzadeh-Mahani, M. and Asadikaram, G., Mohammad Reza Rahbar, M.R. (2017b(. In silico locating the immune-reactive segments of Lepidium draba peroxidase and designing a less immune-reactive enzyme derivative. Computational biology and chemistry 70: 21-30. Gelamo, E.L., Silva, C.H.T.P., Imasato, H. and Tabak, M. (2002). Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modeling. Biochimica et Biophysica Acta 1594: 84–99. Hamid, M. (2009) Potential applications of peroxidases. Food chemistry 15; 115(4):1177-86. Huang, S., Qiu, H., Liu, Y., Huang, C., Sheng, J., Su, W. and Xiao, Q. (2015) Molecular interaction investigation between three CdTe: Zn2+ quantum dots and human serum albumin: a comparative study. Colloids and Surfaces B: Biointerfaces 136: 955-962. Iranfar,H., Rajabi, O., Salari, R., and Chamani, J. (2012). Probing the Interaction of Human Serum Albumin with Ciprofloxacin in the Presence of Silver Nanoparticles of Three Sizes: Multispectroscopic and ζ Potential Investigation, the journal of physical chemistry, J. Phys. Chem. B, 116, 1951−1964 Kandagal, P.B., Shaikh, S.M.T., Manjunatha, D.H., Seetharamappa, J. and Nagaralli, B.S. (2007). Spectroscopic studies on the binding of bioactive phenothiazinecompounds to human serum albumin. J PhotochemPhotobiol A: Chem 189: 121–7. Kim, S., Lee, J., Jang, S., Lee, H., Sung, D. and Chang, J.H. (2016). High efficient chromogenic catalysis of tetramethylbenzidine with horseradish peroxidase immobilized magnetic nanoparticles. Biochemical Engineering Journal 105: 406-411. Krainer, F.W., Pletzenauer, R., Rossetti, L., Herwig, C., Glieder, A. and Spadiut O. (2014). Purification and basic biochemical characterization of 19 recombinant plant peroxidase isoenzymes produced in Pichia pastoris. Protein expression and purification 95: 104-112. Lakowicz, J.R. (1999). Principles of fluorescence spectroscopy, 2nd edn. New York: Kluwer Academic/Plenum Publishers 368. Lee, W.M., An, Y.J., Yoon, H. and Kweon, H.S. (2008). Toxicity and bioavailability of copper nanoparticles to the terrestrial plants mung bean (Phaseolus radiatus) and wheat (Triticum aestivum): Plant agar test for water-insoluble nanoparticles. Environ Toxicol Chem 27(9): 1915-1921. Mahanthappa, M., Savanur, M.A., Puthusseri, B. and Yellappa, S. (2018). Spectroscopic and electrochemical studies on the molecular interaction between copper sulphide nanoparticles and bovine serum albumin. J Mater Sci 53(1): 202-214. Monica, R.C. and Cremonini R. (2009). Nanoparticles and higher plants. Caryologia 62(2): 161-165. Park, W.J., Choi, K.J., Kim, M.H., Koo, B.H., Lee, J.L. Patil, S., Sandberg, A., Heckert, E., Self, W. and Seal, S. (2007). Protein adsorption and cellular uptake of cerium oxide nanoparticles as a function of zeta potential. Biomaterials 28: 4600-4607. Rabbani, G., Khan, M.J., Ahmad, A., Yusof Maskat, M. and Khan, R.H. (2014). Effect of copper oxide nanoparticles on the conformation and activity of β-galactosidase. Colloids Surf B Biointerfaces 123: 96-105. Riahi-Madvar, A. Ghaseminesab, A. Barzegary-Dehaj, F., Zamani, Z. and Rezaee F. (2021). Investigation of the Fe2O3 nanoparticles interaction with human serum albumin using fluorescence and circular dichroism (CD) techniques. Molecular and Cellular Researches. In Press (in Persian). Riahi-Madvar, A. and Ghaseminesab, A. (2018). Study of the CuO nanoparticles interaction with human serum albumin using fluorescence technique. Molecular and Cellular Researches 30(4): 339-348. (in Persian). Roco MC. (1999). Nanoparticles and nanotechnology. JNR 1: 1-6. Rodrigues, R.C., Ortiz, C., Berenguer-Murcia, A., Torres, R., Roberto Fernández-Lafuente, R. (2013). Modifying enzyme activity and selectivity by immobilization. Chemical Society Reviews 42(15): 6290-6307. Ross, P.D. and Subramania, S. (1981). Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20(11): 3096-102. Roy, S. and Das, T.K. (2014). Spectroscopic studies of interaction between biologically synthesized silver nanoparticles and bovine serum albumin. J Nanosci Nanotechnol 14(7): 4899-4905. Sanei, H., Asoodeh, A., Hamedakbari-Tusi, S. and Chamani, J. (2011). Multi-spectroscopic Investigations of Aspirin and Colchicine Interactions with Human Hemoglobin:Binary and Ternary Systems. J Solution Chem 40: 1905–1931. Saptarshi, S.R., Duschl, A. and Lopata, A.L. (2013). Interaction of nanoparticles with proteins: relation to bio-reactivity of the nanoparticle. J Nanobiotechnol 11(1): 26. Sen, T., Mandal, S., Haldar, S., Chattopadhyay, K. and Patra, A. (2011). Interaction of gold nanoparticle with human serum albumin (HSA) protein using surface energy transfer. The Journal of Physical Chemistry C 115(49): 24037-24044. Volkova, K.D., Kovalska, V.B., Tatarets, A.L., Patsenker, L.D., Kryvorotenko, D.V. and Yarmoluk, S.M. (2007). Spectroscopic study of squaraines as protein-sensitivefluorescent dyes. Dyes Pigments 72: 285–92. Wang, B.X., Li, C.H. and Peng, X.F. (2005). Adsorption of nanoparticles on bubble surface in nano-particle suspension. China Particuology 3: 208-212. Welinder, K.G. (1976). Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11. 1.7). FEBS letters 72(1):19-23. Xie, M., Long, M., Liu, Y., Qin, C. and Wang Y. (2006). Characterization of the interaction between human serum albumin and morin. Biochimica et Biophysica Acta 1760: 1184–91. Yang, Q., Liang, J. and Han, H. (2009). Probing the interaction of magnetic iron oxide nanoparticles with bovine serum albumin by spectroscopic techniques. J Phys Chem B113(30): 10454-10458. Zhou, D., Jin, S., Li, L., Wang, Y. and Weng, N. (2011). Quantifying the adsorption and uptake of CuO nanoparticles by wheat root based on chemical extractions. Journal of environmental sciences. 23(11): 1852-1857
| ||
|
آمار تعداد مشاهده مقاله: 260 تعداد دریافت فایل اصل مقاله: 102 |
||
