Development and Comparison of Experimental Assays to Study Protein/Peptide Adsorption onto Surfaces

Duncan, Michelle R.; Gilbert, Mary T.; Lee, Joanne; Warchol, Mark P.

doi:10.1006/jcis.1994.1238

Cited by 7 publications

(4 citation statements)

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“…The phenomenon of protein adsorption has attracted the attention of scientists from several fields who have used a diverse array of techniques to study the processes involved. Techniques such as iodine 125 ( 125 I) radiolabeling, , cyclic voltammetry, , scanning tunneling microscopy, ellipsometry, and more recently electrochemical impedance spectroscopy , have been employed to investigate the adsorption of proteins on various surfaces.…”

Section: Introductionmentioning

confidence: 99%

Investigation of Ig.G Adsorption and the Effect on Electrochemical Responses at Titanium Dioxide Electrode

et al. 2004

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The adsorption of Immunoglobulin G on a titanium dioxide (TiO(2)) electrode surface was investigated using (125)I radiolabeling and electrochemical impedance spectroscopy (EIS). (125)I radiolabeling was used to determine the extent of protein adsorption, while EIS was used to ascertain the effect of the adsorbed protein layer on the electrode double layer capacitance and electron transfer between the TiO(2) electrode and the electrolyte. The adsorbed amounts of Ig.G agreed well with previous results and showed approximately monolayer coverage. The amount of adsorbed protein increased when a positive potential was applied to the electrode, while the application of a negative potential resulted in a decrease. Exposure to solutions of Ig.G resulted in a decrease of the double layer capacitance (C) and an increase in the charge-transfer resistance (R(2)) at the electrode solution interface. As more Ig.G adsorbed onto the electrode surface, the extent of C and R(2) variation increased. These capacitance and charge-transfer resistance variations were attributed to the formation of a proteinaceous layer on the electrode surface during exposure.

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Section: Introductionmentioning

confidence: 99%

Investigation of Ig.G Adsorption and the Effect on Electrochemical Responses at Titanium Dioxide Electrode

et al. 2004

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“…1). Pioneering works proposed, albeit without success, the use of GF/C glass microfiber membranes previously treated with polybrene as transfer membranes for Western-Blot given that peptides and proteins bound preferentially glass hydrophilic surfaces rather than polypropylene hydrophobic surfaces depending on the ionic strength and the presence of surfactants [26][27][28]. Actually, the glass microfiber GF/C filter is an inert porous membrane (1.2 µm pore size) with low unspecific binding and a capillary flow rate of ~1 cm min -1 .…”

Section: Choice Of An Lft Membrane For Immobilizing Torpedo-electrocy...mentioning

confidence: 99%

NeuroTorp, a lateral flow test based on toxin-receptor affinity for in-situ early detection of cyclic imine toxins

Noirmain

Dano

Hue

et al. 2022

Analytica Chimica Acta

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“…In this article, we systematically quantify the adsorption of the three α-helical cationic membrane-active peptides mastoparan X, melittin, and magainin 2 to the walls of commonly used glass and plastic sample containers. This systematic documentation is performed by use of analytical HPLC, which also previously has been used to study adsorption of peptides to solid surfaces of glass and plastic [ 13 ]. Our results clearly demonstrate that interactions between cationic membrane-active peptides and the surfaces of glass and plastic sample containers represent an issue that should not be underestimated by experimental investigators.…”

Section: Introductionmentioning

confidence: 99%

Adsorption of Cationic Peptides to Solid Surfaces of Glass and Plastic

2015

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Cationic membrane-active peptides have been studied for years in the hope of developing them into novel types of therapeutics. In this article, we investigate an effect that might have significant experimental implications for investigators who wish to study these peptides, namely, that the peptides adsorb to solid surfaces of glass and plastic. Specifically, we use analytical HPLC to systematically quantify the adsorption of the three cationic membrane-active peptides mastoparan X, melittin, and magainin 2 to the walls of commonly used glass and plastic sample containers. Our results show that, at typical experimental peptide concentrations, 90% or more of the peptides might be lost from solution due to rapid adsorption to the walls of the sample containers. Thus, our results emphasize that investigators should always keep these adsorption effects in mind when designing and interpreting experiments on cationic membrane-active peptides. We conclude the article by discussing different strategies for reducing the experimental impact of these adsorption effects.

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Development and Comparison of Experimental Assays to Study Protein/Peptide Adsorption onto Surfaces

Cited by 7 publications

References 0 publications

Investigation of Ig.G Adsorption and the Effect on Electrochemical Responses at Titanium Dioxide Electrode

Investigation of Ig.G Adsorption and the Effect on Electrochemical Responses at Titanium Dioxide Electrode

NeuroTorp, a lateral flow test based on toxin-receptor affinity for in-situ early detection of cyclic imine toxins

Adsorption of Cationic Peptides to Solid Surfaces of Glass and Plastic

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