Extended Stern Model
DOI:
https://doi.org/10.6000/1929-5030.2012.01.01.8Keywords:
Stern model, Electric double layer, double layer capacitance, constant phase element, enzymatic solutionsAbstract
In this paper, a theoretical approach of extended Stern model is formulated to represent the electric double layer (EDL) for biochemical as well as biological samples. The existing Stern model is used for several decades to describe the phenomena of electric double layer of electrode/electrolyte interface. In the conventional stern model the double layer which is formed between the electrode and electrolyte interface is described by double layer capacitance. Using the existing Stern model, the equivalent circuit model is not valid for electrical double layer capacitance of electrode/electrolyte interface in β dispersion range. The protein molecules form chemical coupling and chemical adsorption along with classical ionic bonding with gold electrodes. Thus, the compactness of EDL decreases and the double layer capacitance is replaced by a constant phase element (CPE). In the present paper, a three-electrode based ECIS device was used to measure the impedance of various enzymatic solutions for practical realization of theoretical approach. The results obtained from experimental work, were simulated by equivalent circuit simulator, ZsimpWin to validate the extended Stern model by comparing χ2 value. Finally the electrical parameters were extracted and compared for Stern model and extended Stern model. The results obtained by practical experiment and equivalent circuit simulation showed the effectiveness of extended Stern model over Stern model.
References
[1] Bard AJ, Larry R. Faulkner Electrochemical Methods: Fundamentals and Applications. 2nd ed. New York: John Wiley & Sons 2000.
[2] Hunter RJ. Foundations of colloid science. 2nd ed. New York: Oxford University 2001.
[3] Grimnes S, Martinsen ØG. Bioimpedance and Bioelectricity Basics. 2nd ed. London: Academic Press 2000.
[4] Ding S-J, Chang B-W, Wu C-C, Lai M-F, Chang H-C. Electrochemical evaluation of avidin–biotin interaction on self-assembled gold electrodes. Electrochim Acta 2005; 50: 3660-6. http://dx.doi.org/10.1016/j.electacta.2005.01.011
[5] Dulay S, Lozano-Sánchez P, Iwuoha E, Katakis I, O'Sullivan CK. Electrochemical detection of celiac disease-related antitissue transglutaminase antibodies using thiol based surface chemistry. Biosens Bioelectron 2011; 26: 3852-6. http://dx.doi.org/10.1016/j.bios.2011.02.045
[6] Moulton SE, Barisci JN, Bath A, Stella R, Wallace GG. Studies of double layer capacitance and electron transfer at a gold electrode exposed to protein solutions. Electrochim Acta 2004; 49: 4223-30. http://dx.doi.org/10.1016/j.electacta.2004.03.034
[7] Huang H, Ran P, Liu Z. Impedance sensing of allergen– antibody interaction on glassy carbon electrode modified by gold electrodeposition 2007; 70: 257-62.
[8] Stern O. Zur Theorie der Elektrolytischen Doppelschicht. Z Elektrochem 1924; 30: 508-16.
[9] Franks W, Schenker I, Schmutz P, Hierlemann A. Impedance characterization and modeling of electrodes for biomedical applications. IEEE Trans Biomed Eng 2005; 52: 1295-302. http://dx.doi.org/10.1109/TBME.2005.847523
[10] Pradhan R, Mitra A, Das S. Characterization of electrode/electrolyte interface for bioimpedance study. Proceeding of IEEE Students' Technology Symposium (TechSym) 2011; pp. 275-80.
[11] Wang H, Varghese J, Pilon L. Simulation of electric double layer capacitors with mesoporous electrodes: Effects of morphology and electrolyte permittivity. Electrochim Acta 2011; 56: 6189-97. http://dx.doi.org/10.1016/j.electacta.2011.03.140
[12] Sanabria H, Miller JH Jr. Relaxation processes due to the electrode-electrolyte interface in ionic solutions. Phys Rev E Stat Nonlin Soft Matter Phys 2006; 74: 051505. http://dx.doi.org/10.1103/PhysRevE.74.051505
[13] Taylor DM, Macdonald AG. AC admittance of the metal/insulator/electrolyte interface. J Phys D Appl Phys 1987; 20: 1277. http://dx.doi.org/10.1088/0022-3727/20/10/010
[14] Göpel W, Heiduschka P. Interface analysis in biosensor design. Biosens Bioelectron 1995; 10: 853-83. http://dx.doi.org/10.1016/0956-5663(95)99225-A
[15] Boukamp BA. Equivalent Circuits: Users Manual. 2nd ed. Netherlands. University of Twente 1993.
[16] Cui X, Martin DC. Electrochemical deposition and characterization of poly(3,4-ethylenedioxythiophene) on neural microelectrode arrays. Sens Actuators B Chem 2003; 89: 92-102. http://dx.doi.org/10.1016/S0925-4005(02)00448-3
[17] Richardot A, McAdams ET. Harmonic analysis of lowfrequency bioelectrode behavior. IEEE Trans Med Imaging 2002; 21: 604-12. http://dx.doi.org/10.1109/TMI.2002.800576
[18] McAdams ET, Jossinet J. Physical interpretation of Schwan's limit voltage of linearity. Med Biol Eng Comput 1994; 32: 126- 30. http://dx.doi.org/10.1007/BF02518908
[19] Franks W, Schenker I, Schmutz P, Hierlemann A. Impedance characterization and modeling of electrodes for biomedical applications. IEEE Trans Biomed Eng 2005; 52: 1295-302. http://dx.doi.org/10.1109/TBME.2005.847523
[20] Nigel CV. Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry 2004; 65: 249-59. http://dx.doi.org/10.1016/j.phytochem.2003.10.022
[21] Raba J, Mottola HA. Glucose Oxidase as an Analytical Reagent. Crit Rev Anal Chem 1995; 25: 1-42. http://dx.doi.org/10.1080/10408349508050556
[22] Schwalbe H, Grimshaw SB, Spencer A, et al. A refined solution structure of hen lysozyme determined using residual dipolar coupling data. Protein Sci 2001; 10: 677-88. http://dx.doi.org/10.1110/ps.43301
[23] Springman EB, Angleton EL, Birkedal-Hansen H, Van Wart HE. Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a ""cysteine switch"" mechanism for activation. Proc Natl Acad Sci USA 1990; 87: 364-8. http://dx.doi.org/10.1073/pnas.87.1.364
[24] Fujinaga M, Chernaia MM, Mosimann SC, James MNG, Tarasova NI. Crystal structure of human pepsin and its complex with pepstatin. Protein Sci 1995; 4: 960-72. http://dx.doi.org/10.1002/pro.5560040516
Downloads
Published
How to Cite
Issue
Section
License
Policy for Journals/Articles with Open Access
Authors who publish with this journal agree to the following terms:
- Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
- Authors are permitted and encouraged to post links to their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work
Policy for Journals / Manuscript with Paid Access
Authors who publish with this journal agree to the following terms:
- Publisher retain copyright .
- Authors are permitted and encouraged to post links to their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work .
