EGG WHITE ALBUMIN FORM COMPLEX WITH ASPIRIN AND CAFFEINE AND ITS ROLE AS FREE RADICAL SCAVENGER
DOI:
https://doi.org/10.22159/ajpcr.2018.v11i7.25440Keywords:
Egg white albumin, Complex modeling, Free radical scavengerAbstract
Objective: Egg white protein (ovalbumin) is well known to be freshly consumed in Indonesia as traditional medicine, or it is usually known as Jamu.†Ovalbumin, as well as egg white albumin, is able to form complex compounds with other substances through the formation of weak chemical and physical bonds. The objective of this study is to understand the behavior of ovalbumin as radical scavenger when it binds to antioxidants such as aspirin and caffeine (as a complex).
Methods: In this study, docking sites and ovalbumin as scavenger were studied using computer-modeling software. An ovalbumin was used only for computer modeling, whereas in the wet laboratory, the freeze-drying albumin was used for electron spin resonance (ESR) and Fourier transform-infrared (FTIR) spectroscopy to determine its ability as a scavenger and functional groups, respectively. Albumin solution was applied to measure the viscosity.
Results: The variability of tridimensional structures of aspirin was investigated after binding with ovalbumin. However, these structures cannot be seen clearly on caffeine. The root-mean-square deviation analysis showed that aspirin, as well as caffeine, altered the dynamic conformation of ovalbumin. The complex of aspirin-ovalbumin-caffeine which was treated at a temperature of −70°C showed intermolecular force. ESR results showed that the complex compounds could effectively reduce more free radicals when compared to aspirin or caffeine. The existence of aromatic compounds (as confirmed by FTIR) was useful for the scavenger molecules and chemical interaction occurs. The viscosity of the complex was similar with normal gastric mucus, which associated with radical scavenger.
Conclusion: The characters of albumin when it binds to aspirin and caffeine indicated that scavenging activity of the complex and the viscosity showed an important result to be physiological scavengers of free radicals.ÂÂ
Downloads
References
Davalos A, Miguel M, Bartolome B, Lopez-Fandino R. Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis. J Food Prot 2004;67:1939-44.
Kovacs-Nolan J, Phillips M, Mine Y. Advances in the value of eggs and egg components for human health. J Agric Food Chem 2005;53:8421 31.
Walker V, Taylor WH. Ovalbumin digestion by human pepsins 1, 3 and 5. Biochem J 1978;176:429-32.
Nyemb K, Jardin J, Causeur D, Guerin-Dubiard C, Dupont D, Rutherfurd SM, et al. Investigating the impact of ovalbumin aggregate morphology on in vitro ovalbumin digestion using label-free quantitative peptidomics and multivariate date analysis. Food Res Int 2014;63:192-202.
Baynes JW, Dominiczak MH. Medical Biochemistry. 2nd ed. Maryland (USA): Mosby Inc; 2004.
Guerrero A, Gonzalez-Correa JA, Arrebola MM, Munoz-Marin J, De La Cuesta FS, De La Cruz JP. Antioxidant effects of a single dose of acetylsalicylic acid and salicylic acid in rat brain slices subjected to oxygen-glucose deprivation in relation with it’s antiplatelet effect. J Neulet 2004;358:153-56.
Khan MF, Bin Rashid R, Rahman MM, Al Faruk MD, Rahman MD, Rashid MA. Effects of solvent polarity on solvation free energy, dipole moment, polarizability, hyperpolarizability and molecular reactivity of aspirin. Int J Pharm Pharm Sci 2017;9:217-21.
Agyemang-Yeboah F, Oppong SY. Caffeine: The wonder compound, chemistry, and properties. Top Ser Health Sci 2013;1:27-37.
Shah KM, Dadhaniya P, Trivedi VR. Effect of caffeine in experimental model of rheumatoid arthritis in rats. Int J Pharm Pharm Sci 2015;7:365 7.
NCBI. Ovalbumin. Available from: https://www.ncbi.nlm.nih.gov 2006.
PubChem. Aspirin. Caffeine. Available from: https://www.pubchem. ncbi.nlm.nih.gov/2006.
Trott O, Olson AJ. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 2010;31:455-61.
Pymol. The PyMol Molecular Graphics System. Version 1.3. Scrodinger: LLC; 2010.
Wallace AC, Laskowski RA, Thornton JM. LIGPLOT: A program to generate schematic diagrams of protein-ligand interaction. Protein Eng 1995;8:127-34.
Krieger E, Darden T, Nabuurs SB, Finkeistein A, Vriend G. Making optimal of empirical energy functions: Force-field parameterization in crystal space. Proteins Struct Funct Bioinf 2004;57:678-83.
Nisbet AD, Saundry RH, Moir AJ, Fothergill LA, Fothergill JE. The complete amino-acid sequence of hen ovalbumin. Eur J Biochem 1981;115:335-45.
Morozov AV, Kortemme T. Potential functions for hydrogen bonds in protein structure prediction and design. Adv Protein Chem 2005;72:1 38.
Lodish H, Berk A, Matsudaira P, Kaiser CA, Krieger M, Scott MP, et al. Molecular Cell Biology. 5th ed. Madison Avenue (NY): WH Freeman and Company; 2004.
Roche M, Rondeau P, Singh NR, Tarnus E, Bourdon E. Edited by barry halliwell. the antioxidant properties of serum albumin. FEBS Lett 2008;582:1783-87.
Guo F, Li SC, Ma W, Wang L. Detecting protein conformational changes in interactions via scaling known structures. J Comput Biol 2013;20: 765-79.
Oliveira FM, Dos Santos EM, Alves AC, Campana-Pereira MA, Ramaldes GA, Cardoso VN, et al. Digestion, absorption and tissue distribution of ovalbumin and palmitoyl-ovalbumin: Impact on immune responses triggered by orally administered antigens. Scand J Immunol 2007;65:139-47.
Fukumoto LR, Mazza G. Assessing antioxidant and prooxidant activities of phenolic compounds. J Agric Food Chem 2000;48:3597 604.
Shimada K, Fujikawa K, Yahara K, Nakamura T. Antioxidative properties of xanthone on the auto oxidation of soybean in cylcodextrin emulsion. J Agric Food Chem 1992;40:945-8.
Soares JR, Dinis TC, Cunha AP, Almeida LM. Antioxidant activity of some extracts of Thymus zygis. Free Radic Res 1997;26:469-78.
Molyneux P. The use of the stable free radical diphenylpicrylhydrazyl (DPPH) for estimating antioxidant activity. Songklanakarin J Sci Technol 2004;26:211-9.
Brewer MS. Natural antioxidants: Sources, compounds, mechanisms of action, and potential applications. Compr Rev Food Sci Food Saf 2011;10:221-47.
Turnbull CM, McClure D, Rossi AG, Megson IL. A novel electron paramagnetic resonance-based assay for prostaglandin H synthase-I activity. J Inflamm 2006;3:12.
Polyakov NE, Magyar A, Kispert LD. Photochemical and optical properties of water-soluble xanthophyll antioxidants: Aggregation vs complexation. J Phys Chem B 2013;117:10173-82.
Alvarez HA, Mc Carthy AN, Grigera JR. A molecular dynamics approach to ligand-receptor interaction in the aspirin-human serum albumin complex. J Biophys 2012;2012:642745.
Georgiades P, Pudney PD, Thornton DJ, Waigh TA. Particle tracking microrheology of purified gastrointestinal mucins. Biopolymers 2014;101:366-77.
Curt JR, Pringle R. Viscosity of gastric mucus in duodenal ulceration. Gut 1969;10:931-4.
Repetto MG, Llesuy SF. Antioxidant properties of natural compounds used in popular medicine for gastric ulcers. Braz J Med Biol Res 2002;35:523-34.
Bansil R, Turner BS. Mucin strycture, aggregation, physiological functions and biomedical applications. Curr Opin Colloid Interface Sci 2006;11:164-70.
Published
How to Cite
Issue
Section
The publication is licensed under CC By and is open access. Copyright is with author and allowed to retain publishing rights without restrictions.
