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فعالیت ضد آمیلوئیدی عصاره برگ گیاه مرزه (Satureia hortensis L.) روی فیبری شدن لیزوزیم و تأثیر احتمالی آن در درمان بیماریهای وابسته به آمیلوئید | ||
| تحقیقات گیاهان دارویی و معطر ایران | ||
| مقاله 10، دوره 32، شماره 5 - شماره پیاپی 79، دی 1395، صفحه 844-856 اصل مقاله (435.61 K) | ||
| نوع مقاله: مقاله پژوهشی | ||
| شناسه دیجیتال (DOI): 10.22092/ijmapr.2016.108082 | ||
| نویسندگان | ||
| حسن رامشینی* 1؛ نیره کوثری2؛ اعظم السادات مقدسی3 | ||
| 1استادیار بیوشیمی، گروه علمی زیست‌شناسی، دانشگاه پیام نور، تهران، ایران | ||
| 2کارشناسی ارشد، دانشگاه علوم پزشکی سبزوار، بیمارستان مبینی، سبزوار، ایران | ||
| 3کارشناسی ارشد، گروه علمی زیست‌شناسی، دانشگاه آزاد اسلامی، واحد دامغان، ایران | ||
| چکیده | ||
| تجمعات آمیلوئیدی از ویژگی‌های تعداد زیادی از بیماریهای تحلیل برنده سیستم عصبی ازجمله آلزایمر است. بنابراین مهار این تجمعات یک راهکار جذاب برای درمان این بیماری است. به‌طوری که با وجود تحقیقات گسترده‌ای که انجام شده است، یک روش درمانی مؤثر که به‌طور مستقیم باعث مهار این تجمعات گردد تاکنون کشف نشده است. یکی از روش‌های درمانی مهم برای جلوگیری از بروز این بیماری‌ها استفاده از گیاهان دارویی (غنی از ترکیب‌های آروماتیک) می‌باشد. در این مطالعه فعالیت مهاری عصاره برگ گیاه مرزه (Satureia hortensis L.) روی روند فیبریلاسیون لیزوزیم سفیده تخم‌مرغ مورد مطالعه قرار گرفته است. لیزوزیم با غلظت 2 میلی‌گرم بر میلی‌لیتر در بافر گلایسین 50 میلی‌مولار با 5/2pH= تهیه و در دمای 57 درجه به‌طوری که مدام هم زده می‌شود تبدیل به فیبر شد. برای اثبات تشکیل فیبرها از تکنیک‌های مختلفی ازجمله سنجش تیوفلاوین T، فلورسانس خارجی و عکس میکروسکوپ نیروی اتمی استفاده شد. تحلیل داده‌ها با استفاده از آزمون آماری تی مستقل و با نرم‌افزار SPSS.16 انجام گردید.در غیاب عصاره مرزهبعد از 48 ساعت انکوباسیون فیبرهای بالغ آمیلوئیدی ظاهر شد. در حضور عصاره در دامنه غلظت 1-25/0 میلی‌گرم بر میلی‌لیتر تشکیل فیبرهای آمیلوئیدی مهار شد. اثر مهاری وابسته به غلظت بود و بهترین غلظت مؤثر 1 میلی‌گرم بر میلی‌لیتر بدست آمد. عصاره روی تمام مراحل تشکیل فیبر شامل فازهای تأخیر، رشد و تعادل تأثیر می‌گذارد. مطالعه سمّیت سلولی به روش MTT در حضور عصاره در مقایسه با عدم حضور آن نشان داد که سمّیت آنها به‌طور معنی‌داری (05/0>P) کاهش می‌یابد. با توجه به نقش مهاری عصاره روی سمّیت سلولی و اثر آن روی تمامی مراحل مختلف تشکیل فیبر می‌توان از آن در آینده به‌عنوان یک مهارکننده احتمالی برای درمان این نوع از بیماری‌ها استفاده کرد. | ||
| کلیدواژه‌ها | ||
| تجمعات آمیلوئیدی؛ عصاره مرزه (Satureia hortensis L.)؛ لیزوزیم سفیده تخم‌مرغ؛ سمّیت سلولی | ||
| عنوان مقاله [English] | ||
| Anti-amyloidogenic activity of Satureja hortensis L. extract on lysozyme fibrillogenesis and its possible influence on amyloidal diseases treatment | ||
| نویسندگان [English] | ||
| H. Ramshini1؛ N. Kovsari2؛ A. Moghaddasi3 | ||
| 1Department of Biology, Payam Noor University, Tehran, Iran | ||
| 2Mobini Hospital, Sabzevar University of Medical Sciences, Sabzevar, Iran | ||
| 3Department of Biology, Azad University, Branch of Damghan, Damghan, Iran | ||
| چکیده [English] | ||
| Amyloid aggregate plaques are the hallmarks of many neurodegenerative disorders including Alzheimer’s disease. Thus, reducing amyloid deposits is an attractive approach to improve the therapeutic arsenal for the diseases. Despite of intensive research carried out, there is no therapeutic agent directed towards inhibition of aggregation formation. One important approach in the development of therapeutics is the use of herbal extracts, which are rich in aromatic small molecules. This study aimed to explore the inhibitory activity of Satureia hortensis extract against the fibril formation of hen egg-white lysozyme. In this experimental study, amyloid fibrillation was formed in hen egg-white lysozyme under acidic conditions at high temperature. Lysozyme (2 mg/mL) was dissolved in glycine buffer 50 mM, pH=2.5 and incubated at 57°C for the specified durations, while being gently stirred. Various techniques including thioflavin T, ANS fluorescence assay, and atomic force microscopy were used to confirm fibrillation. Data were analyzed through SPSS 16 using descriptive statistics as well as independent t-test.In the absence of Satureia hortensis, mature amyloid aggregates became evident after 48 hours of incubation but upon incubation with various extract concentrations (ranging from 0.25 to 1 mg/ml), formation of amyloid fibrils and oligomers was inhibited. The inhibition was dose-dependent and the best concentration was 1 mg/ml. Our results showed that, the extract was effective in all of amyloid formation processes including lag, polymerization, and equilibrium phases. Also, cytotoxicity of oligomers in the presence of the extract significantly (P<0.05) decreased, as indicated by the MTT assay. Based on inhibitory role of the extract on cytotoxicity of amyloid fibers and its inhibitory effect on all processes of amyloid aggregation, it could be used as a novel inhibitor for Alzheimer's disease. | ||
| کلیدواژه‌ها [English] | ||
| Amyloid aggregation, Satureia hortensis extract, hen egg-white lysozyme, Cytotoxicity | ||
| مراجع | ||
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- Alkam, T., Nitta, A., Mizoguchi, H., Itoh, A. and Nabeshima, T., 2007. A natural scavenger of peroxynitrites, rosmarinic acid, protects against impairment of memory induced by Abeta (25-35). Behavioural Brain Research, 180: 139-145. - Azizi, Z., Ebrahimi, S., Saadatfar, E., Kamalinejad, M. and Majlessi, N., 2012. Cognitive-enhancing activity of thymol and carvacrol in two rat models of dementia. Behavioural Pharmacology, 23: 241-249. - Burley, S.K. and Petsko, G.A., 1985. Aromatic-aromatic interaction: A mechanism of protein structure stabilization. Science, 229: 23-28. - Canale, C., Torrassa, S., Rispoli, P., Relini, A., Rolandi, R., Bucciantini, M., Stefani, M. and Gliozzi, A., 2006. Natively folded HypF-N and its early amyloid aggregates interact with phospholipid monolayers and destabilize supported phospholipid bilayers. Biophysical Journal, 91(12): 4575-4588. - Chiti, F. and Dobson, C.M., 2006. Protein misfolding, functional amyloid, and human disease. Annual Review of Biochemistry, 75: 333-366. - Chromy, B.A., Nowak, R.J., Lambert, M.P., Viola, K.L., Chang, L., Velasco, P.T., Jones, B.W., Fernandez, S.J., Lacor, P.N., Horowitz, P., Finch, C.E., Krafft, G.A. and Klein, W.L., 2003. Self-assembly of Aβ1- 42 into globular neurotoxins. Biochemistry, 42(44): 12749-12760. - Estrada, L.D. and Soto, C., 2007. Disrupting beta-amyloid aggregation for Alzheimerdisease treatment. Current Topics in Medicinal Chemistry, 7: 115-126. - Gertz, H. and Kiefer, M., 2004. Review about Ginkgo biloba special extract EGb 761 (Ginkgo). Current Pharmaceutical Design, 10: 261-264. - Greenwald, J. and Riek, R., 2010. Biology of amyloid: structure, function, and regulation. Structure, 18(10): 1244-1260. - Haass, C. and Selkoe, D.J., 2007. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid beta-peptide. Nature Reviews Molecular Cell Biology, 8: 101-112. - Ho, Y.S., So, K.F. and Chang, R.C., 2010. Anti-aging herbal medicine-how and why can they be used in aging-associated neurodegenerative diseases? Ageing Research Reviews, 9: 354-362. - Hosseinzadeh, H. and Ziaei, T., 2006. Effects of Crocus sativus stigma extract and its constituents, crocin and safranal, on intact memory and scopolamine-induced learning deficits in rats performing the morris water maze task. Journal of Medicinal Plants, 5(19): 3: 40-50. - Hunter, C.A., Lawson, K.R., Perkins, J. and Urch, C.J., 2001. Aromatic interactions. Journal of the Chemical Society Perkin Transactions2, 5: 651-669. - Kheirbakhsh, R., Chinisaz, M., Khodayari, S., Amanpour, S., Dehpour, AR., Muhammadnejad, A., Larijani, B. and Ebrahim-Habibi, A., 2015. Injection of insulin amyloid fibrils in the hippocampus of male Wistar rats: report on memory impairment and formation of amyloid plaques. Neurological Sciences, 36(8): 1411-1416. - Lieberman, H.R., 2001. The effects of ginseng, ephedrine, and caffeine on cognitive performance, mood and energy. Nutrition Reviews, 59: 91-102. - Mattson, M.P., 2000. Apoptosis in neurodegenerative disorders. Nature Reviews Molecular Cell Biology, 1: 120-129. - Mihajilov-Krstev, T., Radnović, D., Kitić, D., Zlatković, B., Ristić, M. and Branković, S., 2009. Chemical composition and antimicrobial activity of Satureja hortensis L. Central European Journal of Biology, 4: 411-416. - Morozova-Roche, L.A., Zurdo, J., Spencer, A., Noppe, W., Receveur, V., Archer, D. B., Joniau, M. and Dobson, C.M., 2000. Amyloid fibril formation and seeding by wild-type human lysozyme and its disease- related mutational variants. Journal of Structural Biology, 130: 339-351. - Nilsson, M.R., 2004. Techniques to study amyloid fibril formation in vitro. Methods, 34: 151-160. - Nordberg, A., 2004. PET imaging of amyloid in Alzheimer's disease. The Lancet Neurology, 3: 519-527. - Porat, Y., Abramowitz, A. and Gazit, E., 2006. Inhibition of amyloid fibril formationby polyphenols: structural similarity and aromatic interactions as a commoninhibition mechanism. Chemical Biology & Drug Design, 67: 27-37. - Ramshini, H., Parrini, C., Relini, A., Zampagni, M., Mannini, B., Pesce, A., Saboury, A.A., Nemat-Gorgani, M. and Chiti, F., 2011. Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils. Plos One, 6: e16075. - Ramshini, H., Ebrahim-Habibi, A., Aryanejad, S. and Rad, A., 2015a. Effect of Cinnamomum verum extract on the amyloid formation of hen egg-white lysozyme and study of its possible role in Alzheimer’s disease. Basic and Clinical Neuroscience, 6: 29-37. - Ramshini, H., Mohammad-Zadeh, M. and Ebrahim-Habibi, A., 2015b. Inhibition of amyloid fibril formation and cytotoxicity by a chemical analog of Curcumin as a stable inhibitor. International Journal of Biological Macromolecules, 78: 396-404. - Ramshini, H. and Ayoubi, F., 2014. Inhibitory effect of Cinnamomum zeylanicum and Camellia sinensis extracts on the hen egg-white lysozyme fibrillation. Journal of Kerman University of Medical Sciences, 21: 290-301. - Rietveld, A. and Wiseman, S., 2003. Antioxidant effects of tea: Evidence from human clinical trials. Journal of Nutrition, 133(10): 3285S-3292S. - Siahmard, Z., Alaei, H., Reisi, P. and Pilehvarian, A.A., 2012. Evaluation of the effects of red grape juice on Alzheimer's disease in rat. Journal of Isfahan Medical School, 29(167): 2383-2390. - Sipe, J.D., Benson, M.D., Buxbaum, J.N., Ikeda, S., Merlini, G., Saraiva, M.J. and Westermark, P., 2010. Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis. Amyloid, 17: 101-104. - Soto, C., Sigurdsson, E.M., Morelli, L., Kumar, R.A., Castaño, E.M. and Frangione, B., 1998. βsheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer’s therapy. Nature Medicine, 4: 822-826. - Tamtaji, O.R., Taghizadeh, M., Takhtfiroozeh, S.M. and Talaei, S.A., 1993. The effect of Elaeagnus angustifolia water extract on scopolamine-induced memory impairment in rats. Journal of Zanjan University of Medical Sciences, 22: 101-111. - Tatini, F., Pugliese, A.M., Traini, C., Niccoli, S., Maraula, G., Ed Dami, T., Mannini, B., Scartabelli, T., Pedata, F., Casamenti, F. and Chiti, F. 2013. Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N. Neurobiol of Aging, 34(9): 2100-2109. - Wang, W., 2005. Protein aggregation and its inhibition in biopharmaceutics. International Journal of Pharmaceutics, 289: 1-30. - Wang, S.S., Liu, K.N. and Lee, W.H., 2009. Effect of curcumin on the amyloid fibrillogenesis of hen egg-white lysozyme. Biophysical Chemistry, 144: 78-87. - Zgorka, G. and Glowniak, K., 2001. Variation of free phenolic acids in medicinal plants belonging to Lamiaceae family. Journal of Pharmaceutical and Biomedical Analysis, 26: 79-87. | ||
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