Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Research Article

Deciphering the Nature of Caffeic Acid to Inhibit the HSA Aggregation Induced by Glyoxal

Author(s): Waseem Feeroze Bhat*, Azaj Ahmed, Shabeena Abbass, Mohammad Afsar, Bilqees Bano and Akbar Masood

Volume 27, Issue 8, 2020

Page: [725 - 735] Pages: 11

DOI: 10.2174/0929866527666200129105141

Price: $65

Abstract

Background: Under certain circumstances, the path for protein folding deviates and attains an alternative path forming misfolded states, which are the key precursors for protein aggregation. Protein aggregation is associated with variety of diseases and leads to the cytotoxicity. These protein aggregate related diseases have been untreated so far. However, extensive attempts have been applied to develop anti-aggregating agents as possible approaches to overcome protein aggregation. Different types of substances have been reported to halt or decrease the formation of ordered protein aggregates both in vitro and in vivo, such as polyphenols and metal ions.

Objective: In the present study the in vitro aggregation of human serum albumin (HSA) by using a reactive dicarbonyl glyoxal has been investigated, simultaneously an attempt has been done to inhibit the glyoxal (GO) induced aggregation of (HSA) by caffeic acid (CA).

Methods: Different methods have been employed to investigate the process, fluorescence spectroscopy, circular dichroism, cango red binding assay, thioflavin T dye binding, turbidimetric analysis, docking study and transmission electron microscopy.

Results: Results have shown that elevated concentration of GO forms aggregates of HSA, and the activity of CA suggested the possibility of inhibiting the HSA aggregation at higher concentrations, and this compound was found to have an anti-aggregation property.

Conclusion: The present study explained that micro molar concentrations of CA inhibits the aggregation of HSA and showed pronounced anti-aggregation effect at increasing concentrations in the presence of GO which is elevated in diabetic and hyperglycaemia conditions.

Keywords: Aggregation, human serum albumin, glyoxal, glycation, caffeic acid, hyperglycaemia.

Graphical Abstract
[1]
Fazili, N.A.; Bhat, W.F.; Naeem, A. Induction of amyloidogenicity in wild type HEWL by a dialdehyde: Analysis involving multi-dimensional approach. Int. J. Biol. Macromol., 2014, 64, 36-44.
[http://dx.doi.org/10.1016/j.ijbiomac.2013.11.010] [PMID: 24291768]
[2]
Bhat, W.F.; Bhat, S.A.; Bano, B. Evaluation of polyphenols as possible therapeutics for amyloidoses: Comparative analysis of Kaempferol and Catechin. Int. J. Biol. Macromol., 2015, 81, 60-68.
[http://dx.doi.org/10.1016/j.ijbiomac.2015.07.052] [PMID: 26231329]
[3]
Matsunaga, Y.; Zerovnik, E.; Yamada, T.; Turk, V. Conformational changes preceding amyloid-fibril formation of amyloid- beta, prion protein and stefin B; parallels in pH dependence. Med. Chem. Res., 2005, 2, 359-367.
[4]
Forman, M.S.; Trojanowski, J.Q.; Lee, V.M. Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs. Nat. Med., 2004, 10(10), 1055-1063.
[http://dx.doi.org/10.1038/nm1113] [PMID: 15459709]
[5]
Gautam, S.; Karmakar, S.; Batra, R.; Sharma, P.; Pradhan, P.; Singh, J.; Chowdhury, P.K. Polyphenols in combination with β-cyclodextrin can inhibit and disaggregate α- synuclein amyloids under cell mimicking conditions: A promising therapeutic alternative. Biochim. Biophys. Acta, 1865, 2017, 589-603.
[6]
Ramazzotti, M.; Melani, F.; Marchi, L.; Mulinacci, N.; Gestri, S.; Tiribilli, B. Degl’ Innocenti, D. Mechanisms for the inhibition of amyloid aggregation by small ligands. Bioscience Reports, 2016, 36(5)e00385
[7]
Fazili, N.A.; Bhat, I.A.; Bhat, W.F.; Naeem, A. Anti-fibrillation propensity of a flavonoid baicalein against the fibrils of hen egg white lysozyme: Potential therapeutics for lysozyme amyloidosis. J. Biomol. Struct. Dyn., 2016, 34(10), 2102-2114.
[http://dx.doi.org/10.1080/07391102.2015.1108232] [PMID: 26555198]
[8]
Bhat, W.F.; Bhat, I.A.; Bhat, S.A.; Bano, B. In vitro disintegration of goat brain cystatin fibrils using conventional and gemini surfactants: Putative therapeutic intervention in amyloidoses. Int. J. Biol. Macromol., 2016, 93(Pt A), 492-500.
[http://dx.doi.org/10.1016/j.ijbiomac.2016.08.082] [PMID: 27597744]
[9]
Lederer, M.O.; Klaiber, R.G. Cross-linking of proteins by Maillard processes: Characterization and detection of lysine-arginine cross-links derived from glyoxal and methylglyoxal. Bioorg. Med. Chem., 1999, 7(11), 2499-2507.
[http://dx.doi.org/10.1016/S0968-0896(99)00212-6] [PMID: 10632059]
[10]
Jabeen, R.; Saleemuddin, M.; Petersen, J.; Mohammad, A. Inactivation and modification of superoxide dismutase by glyoxal: Prevention by antibodies. Biochimie, 2007, 89(3), 311-318.
[http://dx.doi.org/10.1016/j.biochi.2006.10.015] [PMID: 17175088]
[11]
Pace, C.N.; Vajdos, F.; Fee, L.; Grimsley, G.; Gray, T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci., 1995, 4(11), 2411-2423.
[http://dx.doi.org/10.1002/pro.5560041120] [PMID: 8563639]
[12]
Bhat, W.F.; Bhat, S.A.; Bhat, I.A.; Sohail, A.; Shah, A.; Bano, B. Anti-fibrillogenic and fibril destabilizing effects of metal ions on cystatin fibrils. Process Biochem., 2017, 57, 105-116.
[http://dx.doi.org/10.1016/j.procbio.2017.03.021]
[13]
Trott, O.; Olson, A.J. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading J. Comput. Chem, 2010, 31, 455e461.
[14]
Odani, H.; Shinzato, T.; Matsumoto, Y.; Usami, J.; Maeda, K. Increase in three α,β-dicarbonyl compound levels in human uremic plasma: Specific in vivo determination of intermediates in advanced Maillard reaction. Biochem. Biophys. Res. Commun., 1999, 256(1), 89-93.
[http://dx.doi.org/10.1006/bbrc.1999.0221] [PMID: 10066428]
[15]
Lange, J.N.; Wood, K.D.; Knight, J.; Assimos, D.G.; Holmes, R.P. Glyoxal formation and its role in endogenous oxalate synthesis. Adv. Urol., 2012, 2012819202
[http://dx.doi.org/10.1155/2012/819202] [PMID: 22567004]
[16]
Basta, G.; Schmidt, A.M.; De Caterina, R. Advanced glycation end products and vascular inflammation: Implications for accelerated atherosclerosis in diabetes. Cardiovasc. Res., 2004, 63(4), 582-592.
[http://dx.doi.org/10.1016/j.cardiores.2004.05.001] [PMID: 15306213]
[17]
Chen, H.J.; Chen, Y.C.; Hsiao, C.F.; Chen, P.F. Mass spectrometric analysis of glyoxal and methylglyoxal-induced modifications in human hemoglobin from poorly controlled type 2 diabetes mellitus patients. Chem. Res. Toxicol., 2015, 28(12), 2377-2389.
[http://dx.doi.org/10.1021/acs.chemrestox.5b00380] [PMID: 26517015]
[18]
Barros, A.; Rodrigues, J.A.; Almeida, P.J.; Oliva-Teles, M.T. Determination of glyoxal, methylglyoxal, and diacetyl in selected beer and wine, by HPLC with UV spectrophotometric detection, after derivatization with o-phenylenediamine. J. Liq. Chromatogr. Relat. Technol., 1999, 22, 2061-2069.
[http://dx.doi.org/10.1081/JLC-100101786]
[19]
Ghosh, K.S.; Sahoo, B.K.; Dasgupta, S. Spectrophotometric studies on the interaction between (−)-epigallocatechin gallate and lysozyme. Chem. Phys. Lett., 2008, 452, 193-197.
[http://dx.doi.org/10.1016/j.cplett.2007.12.018]

Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy