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JoVE Journal Chemistry

Chemistry

Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method

Published: April 11, 2020 doi: 10.3791/60526
Automatic Translation
1, 1, 1, 1,2, 1
1Nanotechnology Education and Research Center, South Ural State University, 2Laboratory of Computational Modelling of Drugs, South Ural State University

Summary

The first step in comprehending biomolecule-inorganic solid phase interaction is revealing fundamental physicochemical constants that may be evaluated by establishing adsorption isotherms. Adsorption from the liquid phase is restricted by kinetics, surface capacity, pH, and competitive adsorption, which all should be cautiously considered before setting an adsorption experiment.

Abstract

Fundamentals of inorganic-organic interactions are critically important in the discovery and development of novel biointerfaces amenable for utilization in biotechnology and medicine. Recent studies indicate that proteins interact with surfaces through limited adsorption sites. Protein fragments such as amino acids and peptides can be used for interaction modeling between complex biological macromolecules and inorganic surfaces. During the last three decades, many valid and sensitive methods have been developed to measure the physical chemistry fundamentals of those interactions: isothermal titration calorimetry (ITC), surface plasmon resonance (SPR), quartz crystal microbalance (QCM), total internal reflection fluorescence (TIRF), and attenuated total reflectance spectroscopy (ATR).

The simplest and most affordable technique for the measurement of adsorption is the depletion method, where the change in sorbate concentration (depletion) after contact with solution-dispersed sorbent is calculated and assumed to be adsorbed. Adsorption isotherms based on depletion data provide all basic physicochemical data. However, adsorption from solutions requires longer equilibration times due to kinetic restrictions and sorbents with a high specific surface area, making it almost inapplicable to macroscopic fixed plane surfaces. Moreover, factors such as the instability of sols, nanoparticle aggregates, sorbent crystallinity, nanoparticle size distribution, pH of the solution, and competition for adsorption, should be considered while studying adsorbing peptides. Depletion data isotherm construction provides comprehensive physical chemistry data for literally every soluble sorbate yet remains the most accessible methodology, as it does not require expensive setups. This article describes a basic protocol for the experimental study of peptide adsorption on inorganic oxide and covers all critical points that affect the process.

Introduction

For the last 50 years the interaction between inorganic surfaces and peptides has drawn a lot of attention due to its high importance in material science and medicine. Biomedical research is focused on the compatibility and stability of bioinorganic surfaces, which have direct implications for regenerative medicine, tissue engineering1,2,3, and implantation4,5,6,7. Contemporary bioresponsive devices, such as sensors and actuators, are based on functional proteins immobilized on oxide semiconducting surfaces8,9,10,11,12,13. Modern purification practices for protein production often rely on biomolecule interaction properties in downstream purification and separation14.

Among multiple inorganic oxides, titanium dioxide remains the most utilized in combination with biologically relevant substrates15,16. Research in the area of TiO2-based biointerfaces has concentrated on establishing strong and specific binding of proteins and peptides without changing their biological and structural properties. Ultimately, the major objective is a high surface density layer of biomolecules with high stability and increased functionality that will advance the creation of titanium-based biotechnological and medical applications17.

Titanium and its alloys have been used extensively as a surgical implant material for at least six decades because a surface TiO2 layer with a thickness of a few nanometers is corrosion resistant and exhibits a high level of biocompatibility in many in vivo applications18,19,20. Titanium dioxide is also widely considered an inorganic substrate produced in biomineralization, where nucleation and inorganic phase growth accompanied by proteins and peptides may provide materials with promising catalytic and optical properties21,22,23,24.

Given the high relevance of the interaction between inorganic materials and biomolecules in general and protein-TiO2 interactions in particular, there has been a lot of research to address the manipulation and control of the adsorption of proteins on TiO2. Due to these studies, some fundamental properties of this interaction have been revealed, such as adsorption kinetics, surface coverage, and biomolecule conformation, giving substantial support for further advances in biointerfaces5,13.

However, protein complexity adds considerable restrictions on full determination and understanding of a protein's molecular level interaction with inorganic surfaces. Assuming that the biomolecules interact with the inorganic surfaces through limited sites, some proteins with known structures and amino acid sequences have been reduced to their components-peptides and amino acids-which are studied separately. Some of these peptides have demonstrated significant activity, making them a unique subject of adsorption studies without the need for previous protein separation25,26,27,28,29,30.

Quantitative characterization of peptide adsorption on TiO2 or other inorganic surfaces can be accomplished by means of physical methods that have been adapted specifically for biomolecules for the past few decades. These methods include isothermal titration calorimetry (ITC), surface plasmon resonance (SPR), quartz crystal microbalance (QCM), total internal reflection fluorescence (TIRF), and attenuated total reflectance spectroscopy (ATR), all of which allow for the detection of the adsorption strength by providing key thermodynamic data: The binding constant, Gibbs free energy, enthalpy, and entropy31.

The adsorption of biomolecules to the inorganic material may be accomplished in two ways: 1) ITC as well as the depletion method use particles dispersed in a solution binding to fixed macroscopic surfaces; 2) SPR, QCM, TIRF, and ATR use macroscopic surfaces modified with inorganic material, such as gold-coated glass or metal chips, quartz crystals, zinc sulfide crystals, and PMMA chips, respectively.

Isothermal titration calorimetry (ITC) is a label-free physical method that measures the heat produced or consumed upon titration of solutions or heterogeneous mixtures. Sensitive calorimetric cells detect heat effects as small as 100 nanojoules, making the measurement of adsorption heat on nanoparticle surfaces possible. Thermal behavior of the sorbate during continuous addition- titration, provides a full thermodynamic profile of the interaction revealing enthalpy, binding constant, and entropy at a given temperature32,33,34,35,36.

Surface plasmon resonance (SPR) spectroscopy is a surface-sensitive optical technique based on the measurement of the refractive index of the media in close proximity to the studied surface. It is a real-time and label-free method for monitoring reversible adsorption and adsorbed layer thickness. The binding constant can be calculated from the association and dissociation rates. Adsorption experiments performed at different temperatures may provide information about the temperature dependence of the activation energy and sequentially other thermodynamic parameters37,38,39.

The quartz crystal microbalance (QCM) method measures the change in the oscillating frequency of piezoelectric crystals during the adsorption and desorption processes. The binding constant may be evaluated from the ratio of the adsorption and desorption rate constants. QCM is used for relative mass measurements and therefore, needs no calibration25,27,40. QCM is used for adsorption from both gas and liquid. The liquid technique allows QCM to be used as an analysis tool to describe deposition on variously modified surfaces41.

Total internal reflection fluorescence (TIRF) is a sensitive optical interfacial technique based on the measurement of the fluorescence of adsorbed fluorophores excited with internally reflected evanescent waves. The method allows for the detection of fluorescent molecules covering the surface with thicknesses on the order of tens of nanometers, which is why it is used in the study of macromolecular adsorption on various surfaces42,43. In situ monitoring of the fluorescence dynamics upon adsorption and desorption provide the adsorption kinetics and hence thermodynamic data42,43.

Attenuated total reflectance (ATR) was used by Roddick-Lanzilotta to establish lysine adsorption isotherms based on the lysine spectral bands at 1,600 and 1,525 cm-1. This is the first time that the binding constant for a peptide on TiO2 was determined using an in situ infrared method44. This technique was effective in establishing adsorption isotherms for polylysine peptides45 and acidic amino acids46.

Unlike the abovementioned methods, where the adsorption parameter is measured in situ, in a conventional experiment the amount of the adsorbed biomolecules is measured by the concentration change after the surface contacted the solution. Because the concentration of a sorbate decays in a vast majority of adsorption cases, this method is referred to as the depletion method. Concentration measurements require a validated analytical assay, which may be based on an intrinsic analytical property of the sorbate or based on the labeling47,48,49,50 or derivatization51,52 thereof.

Adsorption experiments using QCM, SPR, TIRF, or ATR require special surface preparation of the chips and sensors used for adsorption studies. Prepared surfaces should be used once and require change upon switching the adsorbate, due to the inevitable hydration of the oxide surface or possible chemisorption of a sorbate. Only one sample at a time can be run using ITC, QCM, SPR, TIRF, or ATR, whereas in the depletion method one can run dozens of samples, for which the quantity is only limited by the thermostat capacity and sorbent availability. This is especially important when processing large sample batches or libraries of bioactive molecules. Importantly, the depletion method does not require costly equipment but solely a thermostat.

However, despite its obvious advantages the depletion method requires complex procedural features that may seem cumbersome. This article presents how to perform a comprehensive physicochemical study of dipeptide adsorption on TiO2 using the depletion method and addresses issues that researchers may face when performing relevant experiments.

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Protocol

1. Preparation of dipeptide stock solutions and dilutions

  1. Preparation of 16 mM dipeptide solution
    1. Place 0.183 g of a dipeptide (Ile-His) (see Table of Materials) in a sterile polymeric test tube, dilute to 35 mL with double-distilled water (DDW), and dissolve at room temperature (RT) under vigorous stirring.
      NOTE: If the dipeptide does not dissolve in DDW while stirring, place the dipeptide solution into an ultrasonic bath and sonicate for a few minutes.
    2. Prepare a 50 mM solution of 2-(N-morpholino)ethanesulfonic acid (MES) buffer by dissolving 0.533 g of dry 2-(N-morpholino)ethanesulfonic acid in 50 mL of DDW in the sterile test tube. Prepare a 50 mM sodium hydroxide solution by dissolving 200 mg of sodium hydroxide in 100 mL of DDW.
    3. Adjust the pH of the predissolved dipeptide solution to 7.4 by carefully adding (microliter titration) 50 mM MES, or 50 mM sodium hydroxide to the 16 mM dipeptide solution, stirring at RT and monitoring the pH with a pH meter. After adjusting the pH, pour the solution into a measuring cylinder, rinse the test tube, and fill the measuring cylinder with DDW to 40 mL to make a final concentration of 16 mM.
  2. Preparation of dipeptide dilutions from 16 mM stock solution
    1. Prepare peptide dilutions with concentrations between 0.4 and 12.0 mM by diluting the 16 mM dipeptide solution with DDW. For example, in order to prepare an 8 mM dipeptide solution, add 7 mL of DDW to 10 mL of the 16 mM dipeptide solution. After dilution, adjust the pH to 7.4 by adding 50 mM MES or 50 mM NaOH drop by drop to the dipeptide solution (see step 1.1.3). After adjusting the pH, pour the solution into a measuring cylinder, rinse the test tube, and fill the measuring cylinder up to 20 mL with DDW to make the dipeptide concentration 8 mM.
      NOTE: Other dilutions of 16 mM dipeptide stock solution with concentrations of 0.4, 0.8, 1.2, 1.6, 2.0, 3.0, 4.0, 8.0, and 12.0 mM, are prepared in accordance with Figure 1. The adjustment of each dipeptide solution pH to 7.4 is described in step 1.1.3.

2. Preparation of titania sol

  1. Prepare a 10 mM solution of MES buffer by dissolving 1.066 g of MES in 500 mL of DDW. Adjust the pH to 7.4 with dry sodium hydroxide upon stirring and monitoring the pH with the pH meter.
  2. Grind 200 mg of nanocrystalline TiO2 in a mortar for at least 5 min (see Table of Materials).
  3. Weigh 40 mg of the ground titanium dioxide nanoparticles into a laboratory flask. Put the flask into the sonication bath (see Table of Materials) using the laboratory stand.
  4. Add 20 mL of 10 mM MES buffer into the flask with TiO2 and sonicate in an ultrasonic bath (5 L, 40 kHz, 120 W) for 20 min.

3. Mixing and thermostating

  1. Set the thermostat (see Table of Materials) to the desired temperatures (i.e., 0.00, 10.00, 20.00, 30.00, or 40.00 °C).
  2. Add 1 mL of the sonicated sol of TiO2 to the marked adsorption vials. Place the marked adsorption vials against corresponding dipeptide dilution in a makeshift flotation device made of extruded polystyrene foam. Place the flotation device with the marked vials and corresponding dipeptide dilutions into the thermostat for at least 5 min.
  3. Add 1 mL of each dipeptide dilution to the corresponding marked adsorption vial, making sure all mixing solutions have the same temperature. Keep the series of obtained adsorption samples on the thermostat at 0.00, 10.00, 20.00, 30.00, or 40.00 °C for 24 h to achieve the adsorption equilibrium.
    NOTE: Cautiously shake all the samples of obtained dispersions prior to putting them into the thermostat.
  4. Occasionally mix the TiO2 dispersions by manually shaking them during thermostating.

4. Filtration of the thermostated samples

  1. In order to avoid temperature-induced reequilibration take out one sample at a time from the thermostat for filtration.
  2. Take a sample of the dipeptide solution from each glass vial with a syringe, through a syringe needle. Remove the needle from the syringe and put on the syringe filter (see Table of Materials) to filter the dipeptide solution into the glass vial. Repeat the filtration with the other samples.
  3. Analyze the filtrate in accordance with section 5.
    NOTE: Do not centrifuge the samples, because it takes a few minutes and may cause a change in the concentration equilibrium.

5. Derivatization and HPLC analysis

  1. Make a 50 mL solution of trifluoroacetic acid (TFA) in acetonitrile. Add 0.34 mL of TFA in the measuring cylinder and adjust the volume of the solution to 50 mL with acetonitrile at RT.
    CAUTION: Work with TFA under a fume hood with exhaust ventilation, because trifluoroacetic acid is harmful when inhaled, causes severe skin burns, and is toxic for aquatic organisms even at low concentrations53.
  2. Prepare the derivatization solution (i.e., Edman reagent54) by placing 299 µL of phenyl isothiocyanate and 347 µL of triethylamine in a graduated cylinder and adjusting the volume of solution to 50 mL with acetonitrile at RT.
  3. Prior to the high-performance liquid chromatography (HPLC) analysis, derivatize the samples with Edman's reagent in the chromatography vials. Mix 400 µL of the sample with 400 µL of Edman's reagent. Heat the sample at 60 °C for 15 min. After heating, neutralize the sample with 225 µL of the TFA solution and wait for a few minutes to cool the sample to RT.
  4. Use HPLC analysis (see Table of Materials) to determine the concentration of the dipeptide solution before and after adsorption. Place the chromatography vials with the analyzed solutions into the HPLC autosampler and start analyzing the samples with the necessary conditions, which are set by the software (see Table of Materials).
    NOTE: The mobile phase consists of 0.1% TFA in deionized water and pure acetonitrile, with acetonitrile gradients from 20-90% at 286 nm for 13 min. Analyze each sample in triplicate. Measure the dipeptide solution concentration using the previously established calibration curve (Figure 2). For chromatography specifications see Shchelokov et al.55.

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Representative Results

Adsorption of a dipeptide on nanocrystalline titanium dioxide was studied at the biocompatible conditions in a temperature range of 0−40 °C. Experimental dipeptide adsorption (A, mmol/g) on the surface of a titanium dioxide was evaluated as

Where C0 and Ce are the dipeptide starting and equilibrium concentrations in millimoles, respectively; V is the volume of a dipeptide solution in liters; and m is the weight of the sorbent in grams.

The measurements of the dipeptide adsorption were data processed using the Henry model. This isotherm model assumes adsorption at relatively low concentrations with the sorbate molecules isolated from each other on a sorbent surface and is suitable for describing the experimental data (Figure 3). Note, however, that this model can only be applied in the case of reversible adsorption, which should be confirmed as well. IR-spectroscopy of the material rinsed multiple times is suitable for this purpose. The obtained equilibrium peptide amounts on the TiO2 and solution are related in accordance with the linear equation:

where KH is Henry's adsorption constant.

The equilibrium binding constant KH was obtained from the slope of the dependence of dipeptide adsorption (A) on the dipeptide equilibrium concentration (Ce). The standard Gibbs free energy (ΔG, kJ/mol) for each temperature T was determined through the Van't Hoff equation:

where R is the ideal gas constant in J/mol*K, and T is the temperature of the adsorption process in Kelvin.

Dipeptide Gibbs free energies determined at each temperature (Figure 4) disclosed enthalpy (ΔH) as an interception of the linear regression with the axis. The regression variable, the entropy of the process (ΔS), was derived from the fundamental equation:

The calculated values of the equilibrium binding constant (KH), standard Gibbs energy (ΔG), enthalpy (ΔH), and entropy (ΔS) for Ile-His are presented in Table 1.

Figure 1
Figure 1: Dilution of the 16 mM dipeptide stock solution. Please click here to view a larger version of this figure.

Figure 2
Figure 2: Calibration curve at different dipeptide concentration. The dipeptide concentrations were between 0.4-16.0 mM. Please click here to view a larger version of this figure.

Figure 3
Figure 3: The dipeptide adsorption isotherms calculated by the Henry model for each temperature. Dipeptide adsorption isotherms at (A) 0 °C (B) 10 °C (C) 20 °C (D) 30 °C, and (E) 40 °C, respectively. The calculated correlation coefficients (R2) fell into a 0.96−0.99 range for all obtained Henry model isotherms. Error bars represent the 95% confidence interval for each sample concentration measured in triplicate. Please click here to view a larger version of this figure.

Figure 4
Figure 4: Dependence of the standard Gibbs free energy of the dipeptide adsorption on temperature. Error bars represent the 95% confidence interval for Gibbs free energy as indirect measurement based on Henry Model. Please click here to view a larger version of this figure.

T, K KH ΔG0, kJ/mol ΔH0, kJ/mol ΔS0, kJ/mol K
273.15 0.32 ± 0.01 2.6 ± 0.0 - 41 ± 9 - 0.16 ± 0.03
283.15 0.25 ± 0.01 3.2 ± 0.1
293.15 0.17 ± 0.06 4.3 ± 0.9
303.15 0.050 ± 0.002 7.6 ± 0.1
313.15 0.037 ± 0.002 8.3 ± 0.1

Table 1: Thermodynamic parameters of dipeptide adsorption.

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Discussion

Adsorption from solutions for isotherm construction requires a longer time for equilibration due to kinetic restrictions and sorbents with a high specific surface area. Moreover, instability of sols, nanoparticle aggregates, crystallinity, nanoparticle size distribution, pH of the solution, and competition for adsorption should be considered while adsorbing amino acids. However, adsorption isotherm construction using the depletion method remains the most available methodology, because it does not require expensive setups, and yet it provides exhaustive physical chemistry data for literally every soluble sorbate.

A distinction has to be made between adsorption modes (i.e., solution dispersed particles or on a fixed surface) when a crystalline material is used as a sorbent. One should expect a substantial difference in the distribution of crystalline faces on macroscopically flat surfaces and on particles. Resulting thermodynamic parameters determined from adsorption of peptides on nanoparticles may not correspond to the thermodynamic parameters of peptide adsorption to macroscopically flat surfaces.

The average amount of peptides adsorbed on the inorganic surfaces is extremely low. At room temperature, this value is about several hundreds of micrograms per square meter28. This small amount of adsorbate requires accurate measurement methods and solids with well-developed surfaces. Therefore, small particle substances with a large specific surface (hundreds of square meters) should be used for adsorption experiments43,56,57,58,59,60.

Peptides are, like proteins, unstable, and retain their functionality at a narrow range of conditions. Adsorption experiments were performed on nanocrystalline titanium dioxide at biocompatible temperatures of 0 °C-40 °C (273.15 K-313.15 K), which are similar to those of a normal, functioning, living organism. Adsorption at higher or lower temperatures are irrelevant and should not be considered for the experiment.

Multifunctional biologically active compounds also exhibit high susceptibility to pH of the media, as it affects the surface charge and therefore Coulomb interactions between charged functional groups61,62,63. The sorbent charge of oxide materials is also pH-dependent due to active proton exchange at the hydrated surface64. In order to establish pH stable conditions for adsorption equilibrium use of a buffer is required. In this study, MES buffer is used for its noncoordinating property65, so it would not compete with the peptide for adsorption on the metal oxide surface, unlike phosphate buffers66.

This recent test of amino acid adsorption shows that the major binding site on the nanoparticle is the surface defect55. Defect distribution on the surface is one of the least controllable features of the nanocrystalline substrates, hence one should use sorbent from the same batch in order to maintain consistency in adsorption studies.

QCM, plasmon resonance, and ITC are genuine methods with subtle sensitivity that in a combination of spectroscopic methods reveal structural peculiarities of the adsorbate during interplay with the surface. However, they do not overcome kinetic restrictions and still require considerable time to achieve adsorption equilibration. Furthermore, only one sample at a time can be processed, which makes batch sample analysis challenging. On the other hand, the depletion method presented is simple and only restricted to the thermostat capacity, making the processing of a large number of samples possible.

The thermostated samples should be filtered as soon as they are removed from the thermostat in order to avoid temperature-induced reequilibration. Although equilibration at a new temperature may take up to a few hours, keeping the adsorption samples at a different temperature should be minimized. Centrifugation of the samples for supernatant separation is also not recommended, because it takes up to a few minutes and may cause a change in the concentration equilibrium. The choice of the filter material depends on the sorbate nature and should reduce possible filter-binding for maximum recovery. It is best to follow vendor instructions and recommendations when choosing specific filters.

Additionally, one should bear in mind that concentration change in the adsorption studies should be monitored using validated quantification method using mass spectrometry, radio-spectroscopy, or UV-visible spectroscopy. The analysis is easy if the adsorbate is spectroscopically active, otherwise additional labeling or derivatization of the adsorbate is required.

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Disclosures

The authors have nothing to disclose.

Acknowledgments

This work was financially supported by the Russian Foundation for Basic Research (Grant No. 15-03-07834-a).

Materials

Name Company Catalog Number Comments
2-(N-Morpholino)ethanesulfonic acid TCI Chemicals 4432-31-9 MES, >98%
Acetonitrile Panreac AppliChem HPLC grade
Chromatography vials glass
Dipeptide Ile-His Bachem 4000894
Double-distilled water DDW was obtained on spot
Heating cleaning bath "Ultrasons-HD" J.P. Selecta 3000865 5 L, 40 kHz, 120 Watts
High-performance liquid chromatograph system equipped with a UV−vis detector Shimadzu, LC-20 Prominence HPLC
Isopropanol Sigma-Aldrich (Merck) 67-63-0 99.70%
LabSolutions Lite Shimadzu 223-60410 Software for high-performance liquid chromatography system
Nanocrystalline TiO2 Pure anatase with at least 99% crystallinity. Average particle size 10.62 ± 3.31 nm. Specific surface 131.9 m2/g (BET). See Langmuir 2019, 35, 538−550, for details.
Phenyl isothiocyanate Acros Organics 103-72-0 PITC, 98%
Reversed-phase Zorbax column ZORBAX LC 150×2.5 mm i.d. with a mean particle size of 5 μm
Syringe filter Vladfilter 25 mm, 0.2 μm pore, cellulose acetate
Test sterile polymeric tube polypropylene
Thermostat TC-502 Brookfield Refrigerating/heating circulating bath with the programmable controller for the sample derivatization
Triethylamine Sigma-Aldrich (Merck) 121-44-8 TEA; 99%
Trifluoroacetic acid Panreac AppliChem 163317 TFA, 99%

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References

  1. Garcia, A. J. Interfaces to Control Cell-Biomaterial Adhesive Interactions. Polymers for Regenerative Medicine. 203, Chapter 71 171-190 (2006).
  2. Mahmood, T. A., et al. Modulation of chondrocyte phenotype for tissue engineering by designing the biologic-polymer carrier interface. Biomacromolecules. 7 (11), 3012-3018 (2006).
  3. Gandavarapu, N. R., Mariner, P. D., Schwartz, M. P., Anseth, K. S. Extracellular matrix protein adsorption to phosphate-functionalized gels from serum promotes osteogenic differentiation of human mesenchymal stem cells. Acta Biomaterialia. 9 (1), 4525-4534 (2013).
  4. Horbett, T. Biological Activity of Adsorbed Proteins. Surfactant Science Series. 110, 393-413 (2010).
  5. Ratner, B. D., Hoffman, A. S., Schoen, F. J., Lemons, J. E. Biomaterials Science: An Introduction to Materials in Medicine. , Elsevier Academic Press/Academic Press. San Diego. (2004).
  6. Jahangir, A. R., et al. Fluorinated surface-modifying macromolecules: Modulating adhesive protein and platelet interactions on a polyether-urethane. Journal of Biomedical Materials Research. 60 (1), 135-147 (2002).
  7. Shen, M., et al. PEO-like plasma polymerized tetraglyme surface interactions with leukocytes and proteins: In vitro and in vivo studies. Journal of Biomaterials Science, Polymer Edition. 13 (4), 367-390 (2002).
  8. Wisniewski, N., Moussy, F., Reichert, W. M. Characterization of implantable biosensor membrane biofouling. Fresenius' Journal of Analytical Chemistry. 366 (6-7), 611-621 (2000).
  9. Geelhood, S. J., et al. Passivating Protein Coatings for Implantable Glucose Sensors: Evaluation of Protein Retention. Journal of Biomedical Materials Research. Part B, Applied Biomaterials. 81, 251-260 (2007).
  10. Knowles, J. R. Enzyme catalysis: not different, just better. Nature. 350 (6314), 121-124 (1991).
  11. Blankschien, M. D., et al. Light-triggered biocatalysis using thermophilic enzyme - Gold nanoparticle complexes. ACS Nano. 7 (1), 654-663 (2013).
  12. Wu, H., et al. Catechol modification and covalent immobilization of catalase on titania submicrospheres. Journal of Molecular Catalysis B: Enzymatic. 92, 44-50 (2013).
  13. Gray, J. J. The interaction of proteins with solid surfaces. Current Opinion in Structural Biology. 14 (1), 110-115 (2004).
  14. Hlady, V., Buijs, J. Protein adsorption on solid surfaces. Current Opinion in Biotechnology. 7 (1), 72-77 (1996).
  15. Kulkarni, M., et al. Titanium nanostructures for biomedical applications. Nanotechnology. 26 (6), 062002 (2015).
  16. Yin, F. Z., Wu, L., Gui Yang, H., Su, H. Y. Recent progress in biomedical applications of titanium dioxide. Physical Chemistry Chemical Physics. 15 (14), 4844-4858 (2013).
  17. Rezania, A., Johnson, R., Lefkow, A. R., Healy, K. E. Bioactivation of metal oxide surfaces. 1. Surface characterization and cell response. Langmuir. 15 (20), 6931-6939 (1999).
  18. Schenk, R. The Corrosion Properties of Titanium and Titanium Alloys. Titanium in Medicine. Brunette, D. M., et al. , Springer-Verlag. Berlin, Germany. 145-170 (2001).
  19. Bozzini, B., et al. An electrochemical impedance investigation of the behaviour of anodically oxidised titanium in human plasma and cognate fluids, relevant to dental applications. Journal of Materials Science: Materials in Medicine. 19 (11), 3443-3453 (2008).
  20. Popa, M. V., et al. Long-term assessment of the implant titanium material - Artificial saliva interface. Journal of Materials Science: Materials in Medicine. 19 (1), 1-9 (2008).
  21. Kim, J. K., et al. Lysozyme-mediated biomineralization of titanium-tungsten oxide hybrid nanoparticles with high photocatalytic activity. Chemical Communications. 50, 12392-12395 (2014).
  22. Suriyaraj, S. P., Selvakumar, R. Room temperature biosynthesis of crystalline TiO2 nanoparticles using Bacillus licheniformis and studies on the effect of calcination on phase structure and optical properties. RSC Advances. 4, 39619-39624 (2014).
  23. Inoue, I., et al. Thermo-stable carbon nanotube-TiO2 nanocompsite as electron highways in dye-sensitized solar cell produced by bio-nano-process. Nanotechnology. 26 (28), 285601 (2015).
  24. Gardères, J., et al. Self-assembly and photocatalytic activity of branched silicatein/silintaphin filaments decorated with silicatein-synthesized TiO2 nanoparticles. Bioprocess and Biosystems Engineering. 39 (9), 1477-1486 (2016).
  25. Chen, H., Su, X., Neoh, K. G., Choe, W. S. QCM-D analysis of binding mechanism of phage particles displaying a constrained heptapeptide with specific affinity to SiO2 and TiO2. Analytical Chemistry. 78 (14), 4872-4879 (2006).
  26. Iucci, G., et al. Peptides adsorption on TiO2 and Au: Molecular organization investigated by NEXAFS, XPS and IR. Surface Science. 601 (18), 3843-3849 (2007).
  27. Gronewold, T. M. A., Baumgartner, A., Weckmann, A., Knekties, J., Egler, C. Selection process generating peptide aptamers and analysis of their binding to the TiO2 surface of a surface acoustic wave sensor. Acta Biomaterialia. 5 (2), 794-800 (2009).
  28. Gitelman, A., Rapaport, H. Bifunctional designed peptides induce mineralization and binding to TiO2. Langmuir. 30 (16), 4716-4724 (2014).
  29. Tada, S., Timucin, E., Kitajima, T., Sezerman, O. U., Ito, Y. Direct in vitro selection of titanium-binding epidermal growth factor. Biomaterials. 35 (11), 3497-3503 (2014).
  30. Micksch, T., Liebelt, N., Scharnweber, D., Schwenzer, B. Investigation of the peptide adsorption on ZrO2, TiZr, and TiO2 surfaces as a method for surface modification. ACS Applied Materials and Interfaces. 6 (10), 7408-7416 (2014).
  31. Limo, M. J., Perry, C. C., Thyparambil, A. A., Wei, Y., Latour, R. A. Experimental Characterization of Peptide-Surface Interactions. Bio-Inspired Nanotechnology: From Surface Analysis to Applications. , 37-94 (2013).
  32. Draczkowski, P., Matosiuk, D., Jozwiak, K. Isothermal titration calorimetry in membrane protein research. Journal of Pharmaceutical and Biomedical Analysis. 87, 313-325 (2014).
  33. Omanovic-Miklicanin, E., Manfield, I., Wilkins, T. Application of isothermal titration calorimetry in evaluation of protein-nanoparticle interactions. Journal of Thermal Analysis and Calorimetry. 127, 605-613 (2017).
  34. Jing, X., et al. Interaction of peptidomimetics with bilayer membranes: Biophysical characterization and cellular uptake. Langmuir. 28 (11), 5167-5175 (2012).
  35. Mizuguchi, C., et al. Effect of phosphatidylserine and cholesterol on membrane-mediated fibril formation by the N-terminal amyloidogenic fragment of apolipoprotein A-I. Scientific Reports. 8 (1), 5497 (2018).
  36. Bisker, G., et al. Insulin Detection Using a Corona Phase Molecular Recognition Site on Single-Walled Carbon Nanotubes. ACS Sensors. 3 (2), 367-377 (2018).
  37. Singh, N., Husson, S. M. Adsorption thermodynamics of short-chain peptides on charged and uncharged nanothin polymer films. Langmuir. 22 (20), 8443-8451 (2006).
  38. Seker, U. O. S., et al. Thermodynamics of engineered gold binding peptides: Establishing the structure-activity relationships. Biomacromolecules. 15 (7), 2369-2377 (2014).
  39. Beutner, R., Michael, J., Schwenzer, B., Scharnweber, D. Biological nano-functionalization of titanium-based biomaterial surfaces: A flexible toolbox. Journal of the Royal Society Interface. 7 (Suppl 1), S93-S105 (2010).
  40. Sultan, A. M., et al. Aqueous Peptide-TiO2 Interfaces: Isoenergetic Binding via Either Entropically or Enthalpically Driven Mechanisms. ACS Applied Materials and Interfaces. 8 (28), 18620-18630 (2016).
  41. Teichroeb, J. H., Forrest, J. A., Jones, L. W., Chan, J., Dalton, K. Quartz crystal microbalance study of protein adsorption kinetics on poly(2-hydroxyethyl methacrylate). Journal of Colloid and Interface Science. 325 (1), 157-164 (2008).
  42. Lok, B. K., Cheng, Y. L., Robertson, C. R. Protein adsorption on crosslinked polydimethylsiloxane using total internal reflection fluorescence. Journal of Colloid And Interface Science. 91 (1), 104-116 (1983).
  43. Nakanishi, K., Sakiyama, T., Imamura, K. On the Adsorption of Proteins on Solid Surfaces, a Common but Very Complicated Phenomenon. Journal of Bioscience and Bioengineering. 91 (3), 233-244 (2001).
  44. Roddick-Lanzilotta, A. D., Connor, P. A., McQuillan, A. J. An In Situ Infrared Spectroscopic Study of the Adsorption of Lysine to TiO2 from an Aqueous Solution. Langmuir. 14, 6479-6484 (1998).
  45. Roddick-Lanzilotta, A. D., McQuillan, A. J. An in situ infrared spectroscopic investigation of lysine peptide and polylysine adsorption to TiO2 from aqueous solutions. Journal of Colloid and Interface Science. 217 (1), 194-202 (1999).
  46. Roddick-Lanzilotta, A., McQuillan, A. An in situ infrared spectroscopic study of glutamic acid and of aspartic acid adsorbed on TiO2: implications for the biocompatibility of titanium. Journal of Colloid and Interface Science. 227 (1), 48-54 (2000).
  47. Chan, B. M. C., Brash, J. L. Adsorption of fibrinogen on glass: reversibility aspects. Journal of Colloid And Interface Science. 82 (1), 217-225 (1981).
  48. van Enckevort, H. J., Dass, D. V., Langdon, A. G. The adsorption of bovine serum albumin at the stainless-steel/aqueous solution interface. Journal of Colloid And Interface Science. 98 (1), 138-143 (1984).
  49. Arnebrant, T., Nylander, T. Sequential and competitive adsorption of β-lactoglobulin and κ-casein on metal surfaces. Journal of Colloid And Interface Science. 111 (2), 529-533 (1986).
  50. Van Dulm, P., Norde, W. The adsorption of human plasma albumin on solid surfaces, with special attention to the kinetic aspects. Journal of Colloid And Interface Science. 91 (1), 248-255 (1983).
  51. Gonçalves, T. Fluorescent labeling of biomolecules with organic probes. Chemical Reviews. 109 (1), 190-212 (2009).
  52. Roth, K. D. W., Huang, Z. H., Sadagopan, N., Watson, J. T. Charge derivatization of peptides for analysis by mass spectrometry. Mass Spectrometry Reviews. 17 (4), 255-274 (1998).
  53. AppliChem, P. Safety Data Sheet According to Regulation (EU) 830/2015 3317 Trifluoroacetic Acid. , http://pub.panreac.com/msds/ing/3317.htm 112 (2018).
  54. Heinrikson, R. L., Meredith, S. C. Amino acid analysis by reverse-phase high-performance liquid chromatography: Precolumn derivatization with phenylisothiocyanate. Analytical Biochemistry. 136 (1), 65-74 (1984).
  55. Shchelokov, A., et al. Adsorption of Native Amino Acids on Nanocrystalline TiO2: Physical Chemistry, QSPR, and Theoretical Modeling. Langmuir. 35 (2), 538-550 (2019).
  56. Fair, B. D., Jamieson, A. M. Studies of Protein Adsorption on Polystyrene Latex Surfaces. Journal of Colloid and Interface Science. 77 (2), 525-534 (1980).
  57. Kim, J. C., Lund, D. B. Adsorption behavior of p-lactoglobulin onto stainless steel surfaces. Journal of Food Processing and Preservation. 21 (607), 303-317 (1997).
  58. Kondo, A., Oku, S., Murakami, F., Higashitani, K. Conformational changes in protein molecules upon adsorption on ultrafine particles. Colloids and Surfaces B: Biointerfaces. 1, 197-201 (1993).
  59. Itoh, H., Nagai, T., Saeki, T., Sakiyama, T., Nakanishi, K. Adsorption of Protein onto Stainless Steel Particle Surface and its Desorption Behavior. Developments in Food Engineering. , 811-813 (1994).
  60. Itoh, H., Nagata, A., Toyomasu, T., Sakiyama, T., Nagai, T. Adsorption of β-Lactoglobulin onto the Surface of Stainless Steel Particles. Bioscience, Biotechnology, and Biochemistry. 59 (9), 1648-1651 (1995).
  61. Mudunkotuwa, I. A., Grassian, V. H. Histidine adsorption on TiO2 nanoparticles: An integrated spectroscopic, thermodynamic, and molecular-based approach toward understanding nano-bio interactions. Langmuir. 30, 8751-8760 (2014).
  62. Pászti, Z., Guczi, L. Amino acid adsorption on hydrophilic TiO2: A sum frequency generation vibrational spectroscopy study. Vibrational Spectroscopy. 50 (1), 48-56 (2009).
  63. Costa, D., Savio, L., Pradier, C. M. Adsorption of Amino Acids and Peptides on Metal and Oxide Surfaces in Water Environment: A Synthetic and Prospective Review. Journal of Physical Chemistry B. 120 (29), 7039-7052 (2016).
  64. Kosmulski, M. The significance of the difference in the point of zero charge between rutile and anatase. Advances in Colloid and Interface Science. 99 (3), 255-264 (2002).
  65. Kandegedara, A., Rorabacher, D. B. Noncomplexing tertiary amines as "better" buffers covering the range of pH 3-11. Temperature dependence of their acid dissociation constants. Analytical Chemistry. 71 (15), 3140-3144 (1999).
  66. Susumu, O., Teruaki, A., Koichi, T. The Adsorption of Basic a-Amino Acids in an Aqeous Solution by Titanium(IV) Oxide. Bulletin of the Chemical Society of Japan. 54, 1595-1599 (1981).

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Short Peptide Adsorption Inorganic Nanoparticles Depletion Method Interplay Of Proteins And Peptides Nanotechnology Biomaterials Biotechnology Physico-chemical Constants Adsorption Isotherms Kinetics Surface Capacity PH Comparative Adsorption Dipeptide Adsorption Solution Dispersed Titanium Dioxide Preparation Features Hidden Risks Sterile Polymeric Test Tube Double Distilled Water Room Temperature Stirring Ultrasonic Bath PH Adjustment
Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method
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Korina, E., Naifert, S., Morozov,… More

Korina, E., Naifert, S., Morozov, R., Potemkin, V., Bol'shakov, O. Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method. J. Vis. Exp. (158), e60526, doi:10.3791/60526 (2020).

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