DOI QR코드

DOI QR Code

Impact of pH on the response of bovine serum albumin to gold surface plasmon resonance chip

소 혈청 알부민의 금 표면 플라즈몬 공명 칩과의 반응에 대한 pH의 영향

  • Sohn, Young-Soo (Department of Biomedical Engineering, Daegu Catholic University)
  • 손영수 (대구가톨릭대학교 의공학과)
  • Received : 2021.09.03
  • Accepted : 2021.09.17
  • Published : 2021.09.30

Abstract

Reactions between gold (Au) surface plasmon resonance (SPR) chips and bovine serum albumin (BSA) dissolved in solutions of different pH were investigated. The charge on the BSA depends on the pH of the solution in which it is dissolved. Thus, dissolving BSA in different pH solutions resulted in different charges of BSA. Among the BSA dissolved in solutions with pH 4.01, 7.4, and 10.01, the SPR response was the highest for BSA dissolved in the solution of pH 4.01. To eliminate the response variation owing to the difference in the refractive indices of the solutions, phosphate buffered saline (PBS) was injected into the system after the reaction of BSA with the Au SPR chip had happened. In this case too, the BSA dissolved in the solution with pH 4.01 exhibited the highest response. This may be attributed to the non-uniform distribution of ionic patches on the BSA, which can induce electrostatic attraction to the surface even though BSA has a positive charge at pH 4.01, and the absolute values of the net charge of BSA at pH 4.01 and 7.4 were very close.

Keywords

Acknowledgement

본 연구는 2019년 대구가톨릭대학교 연구년 중 수행하였다.

References

  1. H. Sipova and J. Homola, "Surface plasmon resonance sensing of nucleic acids: A review", Anal. Chim. Acta, Vol. 773, pp. 9-23, 2013. https://doi.org/10.1016/j.aca.2012.12.040
  2. V. Yesudasu, H. S. Pradhan, and R. Jasvanthbhai Pandya, "Recent progress in surface plasmon resonance based sensors: A comprehensive review", Heliyon, Vol. 7, pp. e06321(1)-e06321(13), 2021.
  3. Q. Wang and Z. Liu, "Recent progress of surface plasmon resonance in the development of coronavirus disease-2019 drug candidates", Eur. J. Med. Chem. Rep., Vol. 1, pp. 100003(1)-100003(10), 2021.
  4. P. Falkowski, Z. Lukaszewski, and E. Gorodkiewicz, "Potential of surface plasmon resonance biosensors in cancer detection", J. Pharm. Biomed. Anal., Vol. 194, pp. 113802(1)-113802(11), 2020. https://doi.org/10.1016/j.jpba.2020.113802
  5. C. Situ, J. Buijs, M. H. Mooney, and C. T. Elliott, "Advances in surface plasmon resonance biosensor technology towards high-throughput, food-safety analysis", Trends. Analyt. Chem., Vol. 29, No. 11, pp. 1305-1315, 2010. https://doi.org/10.1016/j.trac.2010.09.003
  6. S. B. D. Borah, T. Bora, S. Baruah, and J. Dutta, "Heavy metal ion sensing in water using surface plasmon resonance of metallic nanostructures", Groundw. Sustain. Dev., Vol. 1, No. 1-2, pp. 1-11, 2015. https://doi.org/10.1016/j.gsd.2015.12.004
  7. R. D. Knight, Physics for Scientists and Engineers (4th/ed.: Korean language edition), Cheong Moon Gak Publishing Company, Gyeonggi-do, pp. 464-1047, 2019.
  8. L. Stryer, Biochemistry (4th/ed.), New York, W. H. Freeman and Company, NY, p. 48, 1995.
  9. B. E. Givens, N. D. Diklich, J. Fiegel, and V. H. Grassian, "Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle-protein interactions", Biointerphases, Vol. 12, No. 2, pp. 02D404(1)-02D404(9), 2017. https://doi.org/10.1116/1.4982598
  10. H. T. M. Phan, S. Bartelt-Hunt, K. B. Rodenhausen, M. Schubert, and J. C. Bartz, "Investigation of bovine serum albumin (BSA) attachment onto self-assembled monolayers (SAMs) using combinatorial quartz crystal microbalance with dissipation (QCM-D) and spectroscopic ellipsometry (SE)", PLoS One, Vol. 10, No. 10, pp. e0141282(1)-e0141282(20), 2015. https://doi.org/10.1371/journal.pone.0141282
  11. T. Kopac, K. Bozgeyik, and J. Yener, "Effect of pH and temperature on the adsorption of bovine serum albumin onto titanium dioxide", Colloids Surf. A Physicochem. Eng. Asp., Vol. 322, pp. 19-28, 2008. https://doi.org/10.1016/j.colsurfa.2008.02.010
  12. H. Kim, C. D. Kim, and Y. S. Sohn, "Characteristics of a bimetal-layer chip of a surface plasmon resonance sensor in the intensity interrogation for tumor marker detection", J. Sens. Sci. Technol., Vol. 25, No. 4, pp. 243-246, 2016. https://doi.org/10.5369/JSST.2016.25.4.243
  13. https://imagej.nih.gov/ij/ (retrieved on Aug. 30, 2021).
  14. W. C. Lee, J. S. Ko, and H. M. Kim, "Effect of electrostatic interaction on the adsorption of globular proteins on octacalcium phosphate crystal film", J. Colloid Interface Sci., Vol. 246, No. 1, pp. 70-77, 2002. https://doi.org/10.1006/jcis.2001.8026
  15. M. Alkan, O. Demirbas, M. Dogan, and O. Arslan, "Surface properties of bovine serum albumin - adsorbed oxides: Adsorption, adsorption kinetics and electrokinetic properties", Microporous Mesoporous Mater., Vol. 96, No. 1-3, pp. 331-340, 2006. https://doi.org/10.1016/j.micromeso.2006.07.007
  16. V. Lesins and E. Ruckenstein, "Protein coated adsorbents for use in potential barrier chromatography: Fouling chromatography", Biotechnol. Prog., Vol. 4, No. 1, pp. 12-24, 1988. https://doi.org/10.1002/btpr.5420040104
  17. V. L. Vilker, C. K. Colton, and K. A. Smith, "The osmotic pressure of concentrated protein solutions: Effect of concentration and pH in saline solutions of bovine serum albumin", J. Colloid Interface Sci., Vol. 79, No. 2, pp. 548-566, 1981. https://doi.org/10.1016/0021-9797(81)90106-5
  18. D. Fologea, B. Ledden, D. S. McNabb, and J. Li, "Electrical characterization of protein molecules by a solid-state nanopore", Appl. Phys. Lett., Vol. 91, pp. 053901(1)-053901(3), 2007. https://doi.org/10.1063/1.2767206