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www.nature.com/scientificreports/ HSA structure57. Native HSA showed spectra at 1660.80 and 1547.0 cm−1 in the Amide I and II region, respec- tively. The change in band position and increase in transmission in MG-HSA was due to the HSA reaction with MG (Fig. 6B), which indicates that the altered secondary structural elements evolved due to the glycation reac- tion. As in the presence of 0.18 and 0.27 mM AgNPs in MG-HSA solution, transmission and band positions (amide I & II) showed minimal changes relative to the 0.09 mM AgNP and MG-HSA reaction mixtures, indicat- ing more unaffected amide bonds and amino groups were present in the solution containing AgNPs58. The change in peak positions in the amide I & II regions and transmittance in FTIR spectroscopy demonstrated a change in the secondary structure of HSA after modification with MG. However, the effects of MG on HSA secondary structure were found to gradually decrease with increasing concentrations of AgNPs. Thus, CD and FTIR analysis of the MG-HSA mixture with and without AgNPs corroborate that AgNPs play an important role in maintaining the secondary structure of HSA protein. Amino acids containing free amino groups (Lys, Arg) are potent sites for glycation in addition to the N-terminal amino acid. AgNPs competitively bind to these free amino groups. These observations gives an indi- cation of decrease in the glycation upon masking of the free amino groups or sequestration of reacting group of glycating agents by AgNPs (e.g., those residing on the lysine residues)59,60. However, the exact mechanism of action of AgNPs is still not clear. In summary, the results of our study indicate that (i) AgNPs can reduce the rate of non-enzymatic modification of HSA by MG and (ii) AgNPs can change the secondary structure of HSA in a concentration independent manner. Conclusion The search for anti-glycating agents is an important clinical issue, as reactive carbonyl entities such as MG, glyoxal and 3-DG are increasingly impacting biological components such as proteins and DNA of the cellular system. In the past, medicinal plants were primarily explored for their anti-oxidant potential. Now, these organisms are being investigated for the presence of novel inhibitors that can nullify the effect of AGEs and help remove the threat posed by these reactive carbonyls that eventually leads to glycation. Several studies have revealed a broad range of potential antibacterial, antimicrobial, anticancer and anti-oxidative activity of AgNPs. Additionally, AgNPs have been shown to interact with the HIV-1 virus and inhibit its ability to bind host cells3. Therefore, AgNPs are believed to have the potential for application for the treatment of several diseases. The results of our present study illustrate that biosynthesized AgNPs have potential anti-glycating ability that may enable their use as therapeutics in the treatment of diabetes related complications. However, a systematic and comprehensive study of the mechanism and the downstream pathways is required before we can expect a more meaningful role of nanoparticles in medicinal applications. References 1. Ashraf, J. M., Arif, B. & Dixit, K., Moinuddin & Alam, K. Physicochemical analysis of structural changes in DNA modified with glucose. Int. J. Biol. Macromol. 51, 604–611 (2012). 2. Ashraf, J. M. et al. 3-Deoxyglucosone: A Potential glycating agent accountable for structural alteration in H3 histone protein through generation of different AGEs. PLoS ONE 01, e0116804. doi: 10.1371/journal.pone.0116804 (2015). 3. Arfat, M. Y., Ashraf, J. M. & Arif, Z., Moinuddin & Alam K. Fine characterization of glucosylated human IgG by biochemical and biophysical methods. Int. J. Biol. Macromol. 69, 408–415 (2014). 4. Baynes, John W. & Vincent M. Monnier. In: The Maillard Reaction in Aging, Diabetes, and Nutrition: Proceedings of an NIH Conference on the Maillard Reaction in Aging, Diabetes, and Nutrition, Held in Bethesda, Maryland, September 22–23, 1988. Vol. 304 (Alan R. Liss, 1989). 5. Ashraf, J. M., Ansari, M. A., Choi, I., Khan, H. M. & Alzohairy, M. A. Antiglycating potential of gum arabic capped-silver nanoparticles. Appl. Biochem. Biotechnol. 174, 398–410 (2014). 6. Monnier, V. M., Stevens, V. J. & Cerami, A. Maillard reactions involving proteins and carbohydrates in vivo: relevance to diabetes mellitus and aging. Prog. Food Nutr. Sci. 5, 315–327 (1981). 7. Phillips, S. A., Mirrlees, D. & Thornalley, P. J. Modification of the glyoxalase system in streptozotocin-induced diabetic rats. Effect of the aldose reductase inhibitor Statil. Biochem. Pharmacol. 46, 805–811 (1993). 8. Papoulis, A., Al-Abed, Y. & Bucala, R. Identification of N2-(1-carboxyethyl)guanine (CEG) as a guanine advanced glycosylation end product. Biochemistry 34, 648–655 (1995). 9. McLellan, A. C., Thornalley, P. J., Ben, J. & Sonksen, P. H. Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clin. Sci. 87, 21–29 (1994). 10. Monnier, V. M., Sell, D. R., Miyarta, S. & Nagaraj, R. H. In: The Maillard Reaction in Food Processing, Human Nutrition, and Physiology (eds Finot, P. A. et al.) pp. 393 (Birkhuser, Basel. 1990). 11. Westwood, M. E., McLellan, A. C. & Thornalley, P. J. Receptor-mediated endocytic uptake of methylglyoxal-modified serum albumin. Competition with advanced glycation end product-modified serum albumin at the advanced glycation end product receptor. J. Biol. Chem. 269, 32293–32298 (1994). 12. Garay-Sevilla, M. E. et al. Advanced glycosylation end products in skin, serum, saliva and urine and its association with complications of patients with type 2 diabetes mellitus. J. Endocrinol. Invest. 28, 223–230 (2005). 13. Brownlee, M., Vlassara, H., Kooney, A., Ulrich, P. & Cerami, A. Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking. Science 232, 1629–1632 (1996). 14. Huby, R. & Harding, J. J. Non-enzymic glycosylation (glycation) of lens proteins by galactose and protection by aspirin and reduced glutathione. Exp. Eye. Res. 47, 53–59 (1988). 15. Booth, A. A., Khalifah, R. G. & Hudson, B. G. Thiamine pyrophosphate and pyridoxamine inhibit the formation of antigenic advanced glycation end-products: comparison with aminoguanidine. Biochem. Biophys. Res. Commun. 220, 113–119 (1996). 16. Malone, J. I., Lowitt, S. & Cook, W. R. Nonosmotic diabetic cataracts. Pediatr. Res. 27, 293–296 (1990). 17. Morimitsu, Y., Yoshida, K., Esaki, S. & Hirota, A. Protein glycation inhibitors from thyme (Thymus vulgaris). Biosci. Biotechnol. Biochem. 59, 2018–2021 (1995). 18. Raza, K. & Harding, J. J. Non-enzymic modification of lens proteins by glucose and fructose: effects of ibuprofen. Exp. Eye Res. 52, 205–212 (1991). 19. Cai, W. & Chen, X. Nanoplatforms for targeted molecular imaging in living subjects. Small 3, 1840–1854 (2007). 20. Treuel, L., Jiang, X. & Nienhaus, G. U. New views on cellular uptake and trafficking of manufactured nanoparticles. J. R. Soc. Interface 10, 20120939 (2013). Scientific RepoRts | 6:20414 | DOI: 10.1038/srep20414 8PDF Image | Green synthesis of silver nanoparticles inhibitory effects on AGEs
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