ANTIGLYCATION AND ANTIAGGREGATION POTENTIAL OF THYMOQUININE

Year 2019, Volume: 6 Issue: 1, 25 - 33, 31.03.2019

Ahmad Ali , Dinesh Kumar

Abstract

Objectives:
The consequences of Diabetes are manifested due to the accumulation of glucose.
The carbonyl group of sugars reacts with the amino group of proteins leading to
generation of harmful products collectively known as advanced glycation end
products (AGEs). These products have been shown to be involved in the various secondary
complications of Diabetes and neurodegenerative disorders. The present study
involves the assessment of role of Thymoquinone in the process of glycation.

Methods:
The in vitro glycation system
consisted of BSA and glucose and incubated in the presence and absence of
thymoquinone for four weeks at 37 ºC. The amount of glycation products were
measured by standard methods like browning, total AGEs by spectrofluorimetry. The
aggregation of protein was checked by aggregation index and Congo red assays.  The effect of thymoquinone was also checked
on the glycation of DNA and the sample was analyzed by agarose gel
electrophoresis.

Results:
The presence of thymoquinone resulted in the decrease in browning and amount of
total AGEs significantly. There was also a drastic decrease in the
glycation-induced aggregation of BSA and reversal of glycoxidative damage of
DNA in the presence of thymoquinone.

Conclusion:
It can be concluded from these results that thymoquinone is potential
antiglycating agent and it can be used to prevent the glycation-induced damage of
biomolecules.

Keywords

Advanced glycation end-products (AGEs), Antiglycation, Browning, Aggregation, DNA damage

References

• Ahmed, N. (2005). Advanced glycation end products-role in pathology of diabetic complications. Diabetes Res Clin Pract, 67, 3-21.
• Ahmad, S., Khan, M.S., Akhter, F., Khan, M.S., Khan, A., Ashraf, J.M. & Shahab. (2014). Glycoxidation of biological macromolecules: a critical approach to halt the menace of glycation. Glycobiology, 24, 979-990.
• Ahmad, S., Moinuddin, S.U., Khan, M.S., Habeeb, S., Alam, K. & Ali, A. (2014). Glycooxidative damage to human DNA – Neo-antigenic epitopes on DNA molecule could be a possible reason for autoimmune response in type 1 diabetes. Glycobiology, 24, 281-291.
• Ali, A., More, T.A., Hoonjan, A.K. & Sivakami, S. (2017). Antiglycating potential of acesulfame potassium: an artificial sweetener. Appl Physiol Nutr Metab, 42, 1054-1063.
• Ali, B.H., & Blunden, G. (2003). Pharmacological and toxicological properties of Nigella sativa. Phytother Res, 2003, 17, 299–305.
• Ali, A., Sharma, R. & Sivakami, S. (2014). Role of natural compounds in the prevention of DNA and proteins damage by glycation. Bionano Front, 7, 25–30.
• Ali, A. & Sharma, R. (2015). A comparative study on the role of lysine and BSA in glycation-induced damage to DNA. Biosci Bioeng Commun, 1, 38-43.
• Anwar, S., Khan, M.A., Sadaf, A. & Younus, H. (2014). A structural study on the protection of glycation of superoxide dismutase by thymoquinone. Int J Biol Macromol, 69, 476-481.
• Banan, P. & Ali, A. (2016). Preventive effect of phenolic acids on in vitro glycation. Annals Phytomed, 5, 97-102.
• Khan, M.A., Anwar, S., Aljarbou, A.N., Al-Orainy, M., Aldebasi, Y.H., Islam, S. & Younus, H. (2014). Protective effect of thymoquinone on glucose or methyl glyoxal-induced glycation of superoxide dismutase. Int J Biol Macromol, 65, 16–20.
• Khan, M.N. & Gothalwal, R. (2018). Herbal origins provision for non-enzymatic Glycation (NEGs) inhibition. Front Medicinal Chem Drug Dis, 2, 1, 10-15.
• Khader, M. & Eckl, P.M. (2014). Thymoquinone: an emerging natural drug with a wide range of medical applications. Iran J Basic Med Sci, 17, 950-957.
• Kikuchi, S., Shinpo, K., Takeuchi, M., Yamagishi, S., Makita, Z., Sasaki, N., & Tashiro, K. (2003). Glycation - a sweet tempter for neuronal death. Brain Res Rev, 41, 306-323.
• Losso, J.N., Bawadi, H.A. & Chintalapati, M. (2011). Inhibition of the formation of advanced glycation end products by thymoquinone. Food Chem, 128, 55-61.
• Lutterodt, H., Luther, M., Slavin, M., Yin, J.J., Parry, J., Gao, J.M., & Yu, L. (2010). Fatty acid profile, thymoquinone content, oxidative stability, and antioxidant properties of cold-pressed black cumin seed oils. LWT - Food Sci Tech, 43, 1409–1413.
• Najmi, A., Nasiruddin, M., Khan, R.A. & Haque, S.F. (2012). Therapeutic effect of Nigella sativa in patients of poor glycemic control. Asian J Pharm Clin Res, 5, 224-228.
• Pandey, R., Kumar, D. & Ali, A. (2018). Nigella sativa seed extracts prevent the glycation of protein and DNA. CurrPers MAPs, 1, 1-7.
• Poulsen, M.W., Hedegaard, R.V., Andersen, J.M., de Courten, B., Bügel, S., Nielsen, J. & Dragsted, L.O. (2013). Advanced glycation end products in food and their effects on health. Food ChemToxicol, 60, 10-37.
• Rondeau, P., Armenta, S., Caillens, H., Chesna, H. & Bourdon, E. (2007). Assessment of temperature effects on b-aggregation of native and glycated albumin by FTIR spectroscopy and PAGE: Relations between structural changes and antioxidant properties. Arch Biochem Biophys, 460, 141-50.
• Sadowska-Bartosz, I. & Bartosz, G. (2015). Prevention of protein glycation by natural compounds. Molecules, 20, 3309-3334.
• Solati, Z., Baharin, B.S., & Bagheri, H. (2014). Antioxidant Property, Thymoquinone Content and Chemical Characteristics of Different Extracts from Nigella sativa L. Seeds. J Am Oil Chem Soc, 91: 295-300.
• Thornalley, P.J. (2003). Use of aminoguanidine (Pimagedine) to prevent the formation of advanced glycation endproducts. Arch Biochem Biophys, 419, 31–40.
• Zafar, H., Hussain, F., Zafar, S. & Yasmin, R. (2013). Glycation inhibition by Nigella sativa (Linn) – an in vitro model. Asian J Agri Bio, 1, 187-189.