Investigation of the Dynamic Surface Adsorption Process of Mucin Protein in the Air-Water Interface

Document Type : Research Article

Authors
Faezeh Zolfigol 1
Vahid Haddadi-Asl 2
Aliyar Javadi 3
Ali Salehi 3
Babak Karimigobaktappeh 2
1 Department of Polymer Engineering, Amirkabir University of Technology, Tehran, Iran
2 Department of Polymer and color Engineering, Amirkabir University of Technology, Tehran, Iran
3 School of Chemical Engineering, University of Tehran, Tehran, Iran
10.22034/amnc.2024.445982.1262
Abstract
Mucin proteins are essential components of the human respiratory system, playing a crucial role in maintaining controlled permeability through the formation of a reticulated structure and electrical charge (exhibiting high surface activity). In addition to their defensive function against external elements, mucins contribute to the dynamic equilibrium in the upper respiratory tract. This study investigates the role of electrical charge in the performance of mucin proteins by introducing and utilizing the drop profile tensiometry method to measure dynamic surface tension and surface elasticity across a wide range of mucin protein concentrations (ranging from 1 to 1000 nanomolar) in buffered solutions. The measurement results of dynamic surface tension indicate a high absorption rate of these large-molecule proteins at the air-water interface for concentrations exceeding one hundred nanomolar. This observation highlights the rapid formation of a structured protective layer in the respiratory system. The measurement of surface elasticity parameters, utilizing interfacial oscillations at different frequencies, demonstrates elevated values of elasticity within the absorbed structured layer.
Keywords
mucin protein
droplet profile analysis
Surface tension dynamics
surface adsorption kinetics
Interface
Subjects
[1] Contributors, W. (1970, January 1). The immune system. Handle Proxy.
[2] Jiménez, A., Vera, L., Lujan-Montelongo, J. (2021). An Overview of Antivirals for Treating lower respiratory Tract Infections. J. Mex. Chem. Soc., 1(66).
[3] Thiriet, M. (2013). Tissue functioning and remodeling in the circulatory and ventilatory systems, Chapter: Airway Surface Liquid and Respiratory Mucus. Springer New York.
[4] Hill, D. B., Long, R. F., Kissner, W. J., Atieh, E., Garbarine, I. C., Markovetz, M. R., Fontana, N., Christy, M., Habibpour, M., Tarran, R., Forest, M. G., Boucher, R. C., & Button, B. (2018). Pathological mucus and impaired mucus clearance in cystic fibrosis patients result from increased concentration, not altered pH. The European Respiratory Journal, 52(6), 1801297. .https://doi.org/10.1183/13993003.01297-2018
[5] Rubin BK. Physiology of airway mucus clearance. Respir Care. 2002 Jul;47(7):761-8. PMID: 12088546.
[6] Bansil, R., Stanley, E., & Lamont, J. T. (1995). Mucin biophysics. Annual Review of Physiology, 57(1), 635–657. https://doi.org/10.1146/annurev.ph.57.030195.003223
[7] Kim, K., McCracken, K., Lee, B., Shin, C., Jo, M., Lee, C., & Ko, K. (1997). Airway goblet cell mucin: Its structure and regulation of secretion. European Respiratory Journal, 10(11), 2644–2649. https://doi.org/10.1183/09031936.97.10112644
[8] Ahern, K., Rajagopal, I., & Tan, T. (2018). Biochemistry: Free For All.
[9] Holmén, J. M., Karlsson, N. G., Abdullah, L. H., Randell, S. H., Sheehan, J. K., Hansson, G. C., & Davis, C. W. (2004a). Mucins and their O-glycans from human bronchial epithelial cell cultures. American Journal of Physiology-Lung Cellular and Molecular Physiology, 287(4). https://doi.org/10.1152/ajplung.00108.2004
[10] Wardzala, C. L., Wood, A. M., Belnap, D. M., & Kramer, J. R. (2022). Mucins inhibit coronavirus infection in a Glycan-Dependent manner. ACS Central Science, 8(3), 351–360. https://doi.org/10.1021/acscentsci.1c01369
[11] H.N. Harkins, W.D. Harkins, The surface tension of blood serum, and the determination of the surface tension of biological fluids, J. Clin. Invest. 7 (1929) 263–281. https://doi.org/10.1172/JCI100228.
[12] C. Kotsmar, V. Pradines, V.S. Alahverdjieva, E.V. Aksenenko, V.B. Fainerman, V.I. Kovalchuk, J. Krägel, M.E. Leser, B.A. Noskov, R. Miller, Thermodynamics, adsorption kinetics and rheology of mixed protein– surfactant interfacial layers, Adv. Colloid Interface Sci. 150 (2009) 41–54. https://doi.org/10.1016/j.cis.2009.05.002.
[13] A. Maestro, C. Kotsmar, A. Javadi, R. Miller, F. Ortega, R.G. Rubio, Adsorption of β-casein-surfactant mixed layers at the air-water interface evaluated by interfacial rheology, J. Phys. Chem. B. 116 (2012) 4898–4907. https://doi.org/10.1021/jp301031y.
[14] A. Moosavi-Movahedi, J. Chamani, A. Taghavi, H. Moghadamnia, Proteins: Structure and Function, 1st ed., University of Tehran, Tehran, 2004.
[15] Shourni, S., Javadi, A., Hosseinpour, N., Bahramian, A., & Raoufi, M. (2022). Characterization of protein corona formation on nanoparticles via the analysis of dynamic interfacial properties: Bovine serum albumin - silica particle interaction. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 638, 128273. https://doi.org/10.1016/j.colsurfa.2022.
[16] 128273Javadi, A., Mucic, N., Karbaschi, M., Won, J., Lotfi, M., Dan, A., Ulaganathan, V., Gochev, G., Makievski, A. V., Kovalchuk, V. I., Kovalchuk, N. M., Krägel, J., & Miller, R. (2013). Characterization methods for liquid interfacial layers. European Physical Journal-special Topics, 222(1), 7–29. https://doi.org/10.1140/epjst/e2013-01822-3
[17] Javadi, A., Mucic, N., Karbaschi, M., Won, J., Lotfi, M., Dan, A., Ulaganathan, V., Gochev, G., Makievski, A. V., Kovalchuk, V. I., Kovalchuk, N. M., Krägel, J., & Miller, R. (2013b). Characterization methods for liquid interfacial layers. European Physical Journal-special Topics, 222(1), 7–29. https://doi.org/10.1140/epjst/e2013-01822-3
[18] F. Ravera, G. Loglio, V.I. Kovalchuk, Interfacial dilational rheology by oscillating bubble/drop methods, Curr. Opin. Colloid Interface Sci. 15 (2010) 217–228. https://doi.org/10.1016/j.cocis.2010.04.001.
[19] B.C. Tripp, J.J. Magda, J.D. Andrade, Adsorption of Globular Proteins at the Air/Water Interface as Measured via Dynamic Surface Tension: Concentration Dependence, Mass-Transfer Considerations, and Adsorption Kinetics, J. Colloid Interface Sci. 173 (1995) 16–27. https://doi.org/10.1006/jcis.1995.1291.
[20] I. Yadav, V.K. Aswal, J. Kohlbrecher, Size-dependent interaction of silica nanoparticles with lysozyme and bovine serum albumin proteins, Phys. Rev. E. 93 (2016). https://doi.org/10.1103/PhysRevE.93.052601.
[21] S.A. Zholob, A. V. Makievski, R. Miller, V.B. Fainerman, Optimisation of calculation methods for determination of surface tensions by drop profile analysis tensiometry, Adv. Colloid Interface Sci. 134–135 (2007) 322–329. https://doi.org/10.1016/j.cis.2007.04.011.