Abstract
The effects of the anionic surfactant, sodium dodecyl sulfate (SDS), and of the cationic surfactant cetyltrimethylammonium bromide (CTAB) on the gelation kinetics of bovine serum albumin (BSA) hydrogel were investigated by rheological measurements using surfactant concentrations of 0–0.05 M, and BSA concentrations of 5, 7, and 10 wt%. It was found while an increase in CTAB concentration accelerated the rate of gelation of BSA solution under temperature jump and temperature ramp conditions, BSA solutions containing SDS exhibited a heat-dependent protective effect against thermal denaturation and gelation. Under temperature ramp conditions, inhibition of BSA gelation by SDS was diminished by increasing SDS concentration, while under temperature jump conditions, inhibition of BSA gelation increased with SDS concentration. That is, gel temperature (Tgel) under temperature ramp decreased with increasing CTAB and with SDS concentration, but under temperature jump the gel time (tgel) decreased with increasing CTAB concentration but increased with SDS concentration. Furthermore, BSA/CTAB solutions were found to gel more rapidly than BSA/SDS solutions, which was in line with the lower activation energy of BSA/CTAB gel. In support of experiments, molecular dynamics (MD) simulations and dynamic light scattering (DLS) revealed the faster rate of BSA denaturation in the presence of CTAB was responsible for the increased gelation rate of BSA/CTAB solutions, whereas BSA was found to be protected by SDS against thermal denaturation leading to the slower gelation rate of BSA/SDS solutions.
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References
Ahmed J, Ramaswamy HS, Alli I (2006) Thermorheological characteristics of soybean protein isolate. J Food Sci 71:158–163
Berglund KD, Truong MT, Przybycien TM, Tilton RD, Walker LM (2003) Rheology of transient networks containing hydrophobically modified cellulose, anionic surfactant and colloidal silica: role of selective adsorption. Rheol Acta 43:50–61
Bocker L, Ruhs PA, Boni L, Fischer P, Kuster S (2016) Fiber-enforced hydrogels: hagfish slime stabilized with biopolymers including κ-carrageenan. Biomater Sci Eng 2:90–95
Branco MC, Pochan DJ, Wagner NJ, Schneider JP (2010) The effect of protein structure on their controlled release from an injectable peptide hydrogel. Biomaterials 31:9527–9534
Chen J, Hao J (2013) Molecular dynamics simulation of cetyltrimethylammonium bromide and sodium octyl sulfate mixtures: aggregate shape and local surfactant distribution. Phys Chem Chem Phys 15:5563–5571
Chronakis IS (2001) Gelation of edible blue-green algae protein isolate (Spirulina platensis Strain Pacifica): thermal transitions, theological properties, and molecular forces involved. J Agric Food Chem 49:888–898
Czerner M, Fasce LA, Martucci JF, Ruseckaite R, Frontini PM (2016) Deformation and fracture behavior of physical gelatin gel systems. J Food Hyd 60:299–307
Da Silva MA, Areas EP (2005) Solvent-induced lysozyme gels: rheology, fractal analysis, and sol-gel kinetics. J Coll Inter Sci 289:394–401
Date P, Ottoor D (2016) pH dependent controlled release of CTAB incorporated dipyridamole drug from agar-based hydrogel. Polym Plast Technol Eng 55:403–413
De Maria S, Ferrari1 G, Maresca P (2015) Rheological characterization bovine serum albumin gels induced by high hydrostatic pressure. Food Nutr Sci 6:770–779
De Vicente J, Stokes JR, Spikes HA (2006) Soft lubrication of model hydrocolloids. Food Hydr 20:483–491
Dominguez H (2017) Interaction of the interleukin 8 protein with a sodium dodecyl sulfate micele: a computer simulation study. J Mol Model 23:210
Eleya MMO, Gunasekaran S (2002) Gelling properties of egg white produced using a conventional and a low-shear reverse osmosis process. J Food Sci 67:725–729
Goncalves C, Pereira P, Gama M (2010) Self-assembled hydrogel nanoparticles for drug delivery applications. Materials 3:1420–1460
Guo H, Sanson N, Marcellan A, Hourdet D (2016) Thermoresponsive toughening in LCST-type hydrogels: comparison between semi-interpenetrated and grafted networks. Macromolecules 49:9568–9577
Hao J, Weiss RA (2016) Tuning the viscoelastic behavior of hybrid hydrogels composed of a physical and a chemical network by the addition of an organic solvent. Macromolecules 49:6687–6693
Head DA, Briels J, Gompper G (2014) Nonequilibrium structure and dynamics in a microscopic model of thin-film active gels. Phy Rev E 89:032705
Heinig M, Frishman D (2004) STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins. Nucleic Acids Res 32:500–502
Holt JC, Creeth JM (1972) Studies of the denaturation and partial renaturation of ovalbumin. Biochip J 129:665–676
Hyun K, Wilhelm M, Klein CO, Cho KS, Nam JG, Ahn KH, Lee SJ, Ewoldt RH, McKinley GH (2011) A review of nonlinear oscillatory shear tests: analysis and application of large amplitude oscillatory shear (LAOS). Prog Polym Sci 36:1697–1753
Jachimska B, Wasilewska M, Adamczyk Z (2008) Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements. Langmuir 24:6866–6872
Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577–2637
Krishnamani V, Lanyi JK (2012) Molecular dynamics simulation of the unfolding of individual bacteriorhodopsin helices in sodium dodecyl sulfate micelles. Biochemistry 51:1061–1069
Kundu S, Chinchalikar AJ, Das K, Aswal VK, Kohlbrecher J (2013) Fe+3 ion induced protein gelation: small-angle neutron scattering study. Chem Phys Letters 584:172–176
Le Bon C, Nicolai T, Durand D (1999) Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation. Macromolecules 32:6120–6127
Lemkul JA, Allen WJ, Bevan DR (2010) Practical considerations for building GROMOS- compatible small-molecule topologies. J Cheam Inf Model 50:2221–2235
Lohcharoenka W, Wang L, Chen YC, Rojanasakul Y (2014) Protein nanoparticles as drug delivery carriers for cancer therapy. BioMed Res Int 1-12
Madbouly SA, Otaigbe JU (2006) Kinetic analysis of fractal gel formation in waterborne polyurethane dispersions undergoing high deformation flows. Macromolecules 39:4144–4151
Malkin AY, Kulichikhin SG (1996) Rheokinetics: rheological transformation in synthesis and reaction of oligomers and polymers. Heidelberg, Huthing & Wepf Verlag
Meyer M, Morgenstern B (2003) Characterization of gelatine and acid soluble collagen by size exclusion chromatography coupled with multi angle light scattering (SEC-MALS). Biomacromolecules 4:1727–1732
Moriyama Y, Sato Y, Takeda K (1993) Reformation of the helical structure of bovine serum albumin by the addition of small amounts of sodium dodecyl sulphate after the disruption of the structure by urea. J Coll Inter Sci 156:420–424
Moriyama Y, Watanabe E, Kobayachi K, Harano H, Inui E, Takeda K (2008) Secondary structural change of bovine serum albumin in thermal denaturation up to 130 °C and protective effect of sodium dodecyl sulfate on the change. J Phys Chem B 112:16585–16589
Nnyigide OS, Oh Y, Song HY, Park E, Choi S, Hyun K (2017) Effect of urea on heat-induced gelation of bovine serum albumin (BSA) studied by rheology and small angle neutron scattering (SANS). Korea-Aust Rheol J 29:101–113
Nnyigide OS, Lee SG, Hyun K (2018) Exploring the differences and similarities between urea and thermally driven denaturation of bovine serum albumin: intermolecular forces and solvation preferences. J Mol Model 24:75
Nochos A, Douroumis D, Bouropoulos N (2008) In vitro release of bovine serum albumin from alginate/HPMC hydrogel beads. Carbohydr Polym 74:451–457
Oelschlaeger C, Suwita P, Willenbacher N (2010) Effect of counterion binding efficiency on structure and dynamics of wormlike micelles. Langmuir 26:7045–7053
Otzen DE (2002) Protein unfolding in detergents: effect of micelle structure, ionic strength, pH, and temperature. Biophys J 83:2219–2230
Patel A, Cholkar K, Mitra AK (2014) Recent developments in protein and peptide parenteral delivery approaches. Ther Deliv 5:337–365
Pereira C, Bohe J, Rosselli S, Combourieu E, Pommier C, Perdrix J, Richard J, Badet M, Gaillard S, Philit F, Guerin C (2003) Sigmoidal equation for lung and chest wall volume-pressure curves in acute respiratory failure. J Appl Physiol 95:2064–2071
Puppo MC, Anon MC (1998) Effect of pH and protein concentration on rheological behavior of acidic soybean protein gels. J Agric Food Chem 46:3039–3046
Rogozea A, Matei I, Turcu IM, Ionita G, Sahini VE, Salifoglou A (2012) EPR and circular dichroism solution studies on the interactions of bovine serum albumin with ionic surfactants and β-cyclodextrin. J Phys Chem B 116:14245–14253
Salzer S, Rosema NA, Martin EC, Slot DE, Timmer CJ, Dorfer CE, van der Weijden GA (2016) The effectiveness of dentifrices without and with sodium lauryl sulfate on plaque, gingivitis and gingival abrasion— a randomized clinical trial. Clin Oral Invest 20:443–450
Schomaecker R, Robinson BH, Fletcher PDI (1988) Interaction of enzymes with surfactants in aqueous solution and in water-in-oil microemulsions. J Chem Soc Faraday Trans 1(84):4203–4212
Schultz KM, Campo-Deano L, Baldwin AD, Kiick KL, Clasen C, Furst EM (2015) Electrospinning covalently cross-linking biocompatible hydrogelators. Polymer 54:363–371
Singh H, Waungana A (2001) Influence of heat treatment of milk on cheese making properties. Int Dairy J 11:543–551
Storm S, Jakobtorweihen S, Smirnova I, Panagiotopoulos AZ (2013) Molecular dynamics simulation of SDS and CTAB micellization and prediction of partition equilibria with COSMOmic. Langmuir 29:11582–11592
Tichopad A, Dzidic A, Pfaffl MW (2002) Improving quantitative real-time RT-PCR reproducibility by boosting primer-linked amplification efficiency. Biotechnol Lett 24:2053–2056
Tobitani A, Ross-Murphy SB (1997) Heat-induced gelation of globular proteins. 1. Model for the effects of time and temperature on the gelation time of BSA gels. Macromolecules 30:4845–4854
Touw WG, Baakman C, Black J, Tee Beek TA, Krieger E, Joosten RP, Vriend GA (2015) Series of PDB-related databanks for everyday needs. Nucleic Acids Res 43:D364–D368
Valstar A (2000) Protein-surfactant interactions. Ph.D. dissertations, Uppsala University, Uppsala, Sweden
Valstar A, Almgren M, Brown W (2000) The interaction of bovine serum albumin with surfactants studied by light scattering. Langmuir 16:922–927
Van Kleef FSM (1986) Thermally induced protein gelation: gelation and rheological characterization of highly concentrated ovalbumin and soybean protein gels. Biopolymers 25:31–59
Yadav R (2014) Domain specific interactions, unfolding and ultrafast of human and bovine serum albumin: a bulk and single molecular level study. Ph.D. dissertations Indian Institute of Technology Kanpur, Kanpur
Ying H, Zang Y, Cheng J (2014) Dynamic urea bond for the design of reversible and self-healing polymers. Nat Commun 5:3218
Yoshida M, Kohyama K, Nishinari K (1992) Gelation properties of soymilk and soybean 11S globulin from Japanese-grown soybeans. Biosci Biotechnol Biochem 56:725–728
Yu Z, Yu M, Zhang Z, Hong G, Xiong Q (2014) Bovine serum albumin nanoparticles as controlled release carrier for local drug delivery to the inner ear. Nanoscale Res Lett 9:343
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This study was financially supported by the Basic Science Research Program (2015R1D1A1A09057413) through the Research Foundation of Korea (NRF).
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Nnyigide, O.S., Hyun, K. Effects of anionic and cationic surfactants on the rheological properties and kinetics of bovine serum albumin hydrogel. Rheol Acta 57, 563–573 (2018). https://doi.org/10.1007/s00397-018-1100-1
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DOI: https://doi.org/10.1007/s00397-018-1100-1