Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

Grabowska, Ola; Kogut, Małgorzata M.; Żamojć, Krzysztof; Samsonov, Sergey A.; Makowska, Joanna; Tesmar, Aleksandra; Chmur, Katarzyna; Wyrzykowski, Dariusz; Chmurzyński, Lech

doi:10.3390/molecules26216565

Cited by 7 publications

(3 citation statements)

References 44 publications

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“…In aggregate, the data demonstrate the ability of the hydrogels to release DOX in its active form through photothermal modulation. These data together with prior reports of the photothermally induced release of active proteins from hydrogels − and of protein stability up to 60 °C , bode well for the potential of our hydrogels as a delivery system for a wide array of therapeutic agents.…”

Section: Resultssupporting

confidence: 67%

Photothermal Modulation of Dynamic Covalent Poly(ethylene glycol)/PEDOT Composite Hydrogels for On-Demand Drug Delivery

Thapa,

FitzSimons,

Otakpor

et al. 2023

ACS Appl. Mater. Interfaces

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Hydrogels are cross-linked three-dimensional polymer networks that have tissue-like properties. Dynamic covalent bonds (DCB) can be utilized as hydrogel cross-links to impart injectability, self-healing ability, and stimuli responsiveness to these materials. In our research, we utilized dynamic thiol-Michael bonds as cross-links in poly(ethylene glycol) (PEG)-based hydrogels. Because the equilibrium of the reversible, exothermic thiol-Michael reaction can be modulated by temperature, we investigated the possibility of using thermal and photothermal stimuli to modulate the gel-to-sol transition of these materials with the aim of developing an on-demand pulsatile cargo release system. For this purpose, we incorporated poly(3,4-ethylenedioxythiophene) (PEDOT) nanoparticles within the hydrogel to facilitate photothermal modulation using near-infrared light. PEDOT nanoparticles of 50 nm in diameter and with strong near-infrared absorption were prepared by oxidative emulsion polymerization. We then used Michael addition of thiol−ene pairs from 4-arm PEG-thiol (PEG-SH) and 4-arm PEG-benzylcyanoacetamide (PEG-BCA) to form dynamically cross-linked hydrogels. PEDOT nanoparticles were entrapped in situ to form Gel/PEDOT composites. Rheology and inverted tube test studies showed that the gel-to-sol transition occurred at 45−50 °C for 5 wt % gels and that this transition could be tailored by varying the wt % of the polymer precursors. The hydrogels were found to be capable of self-healing and being injected with a clinically relevant injection force. Bovine serum albumin-fluorescein isothiocyanate (BSA-FITC), a fluorescently labeled protein, was then loaded into the Gel/PEDOT as a therapeutic mimic. Increased release of BSA-FITC upon direct thermal stimulation and photothermal stimulation with an 808 nm laser was observed. Pulsatile release of BSA-FITC over seven cycles was demonstrated. MTS and live−dead assays demonstrated that Gel/PEDOT was cytocompatible in MDA-MB-231 breast cancer and 3T3 fibroblast cell lines. Further studies demonstrated that the encapsulation and laser-triggered release of the chemotherapeutic agent doxorubicin (DOX) could also be achieved. Altogether, this work advances our understanding of the temperature-dependent behavior of a dynamic covalent hydrogel, Gel/PEDOT, and leverages that understanding for application as a photothermally responsive biomaterial for controlled release.

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Section: Resultssupporting

confidence: 67%

Photothermal Modulation of Dynamic Covalent Poly(ethylene glycol)/PEDOT Composite Hydrogels for On-Demand Drug Delivery

Thapa,

FitzSimons,

Otakpor

et al. 2023

ACS Appl. Mater. Interfaces

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“…Bovine serum albumin (BSA) is a protein found in bovine blood serum. One of its main features is specific binding sites that have physiological significance for transport, modulation and inactivation of metabolite and drug activities [ 1 , 2 , 3 , 4 ]. BSA is a universal carrier for fatty acids, ions, ligands, hormones and metabolites [ 5 , 6 ].…”

Section: Introductionmentioning

confidence: 99%

Influence of Low Molecular Weight Salts on the Viscosity of Aqueous-Buffer Bovine Serum Albumin Solutions

et al. 2022

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Pharmaceutical design of protein formulations aims at maximum efficiency (protein concentration) and minimum viscosity. Therefore, it is important to know the nature of protein-protein interactions and their influence on viscosity. In this work, we investigated the dependence of the viscosity of BSA in an aqueous 20 mM acetate buffer at pH = 4.3 on protein concentration and on temperature (5–45 ∘C). The viscosity of the solution increased with protein concentration and was 230% higher than the viscosity of the protein-free formulation at 160 mg/mL. The viscosity decreased by almost 60% in the temperature range from 5 to 45 ∘C. The agreement of the modified Arrhenius theory with experiment was quantitative, whereas a hard-sphere model provided only a qualitative description of the experimental results. We also investigated the viscosity of a 100 mg/mL BSA solution as a function of the concentration of added low molecular weight salts (LiCl, NaCl, KCl, RbCl, CsCl, NaBr, NaI) in the range of salt concentrations up to 1.75 mol/L. In addition, the particle size and zeta potential of BSA-salt mixtures were determined for solutions containing 0.5 mol/L salt. The trends with respect to the different anions followed a direct Hofmeister series (Cl- > Br- > I-), whereas for cations in the case of viscosity the indirect Hofmeister series was observed (Li+ > Na+ > K+ > Rb+ > Cs+), but the values of particle sizes and zeta potential did not show cation-specific effects. Since the protein is positively charged at pH = 4.3, anions are more attracted to the protein surface and shield its charge, while the interaction with cations is less pronounced. We hypothesize that salt surface charge shielding reduces protein colloidal stability and promotes protein aggregate formation.

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“…Due to a huge variety of industrial, biological, medical, and technical applications of surfactants in the fields of chemicals, detergents, cosmetics, foods, and pharmaceuticals [ 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 ], their interactions with proteins have been in recent years extensively studied, mainly in terms of factors that determine the association extent as well as modifications of the protein physicochemical and functional properties (in the case of enzymes, transport proteins, and toxins) caused by association-elicited conformational changes [ 11 , 12 , 13 , 14 , 15 , 16 , 17 ].…”

Section: Introductionmentioning

confidence: 99%

On the Effect of pH, Temperature, and Surfactant Structure on Bovine Serum Albumin–Cationic/Anionic/Nonionic Surfactants Interactions in Cacodylate Buffer–Fluorescence Quenching Studies Supported by UV Spectrophotometry and CD Spectroscopy

Żamojć

Wyrzykowski

Chmurzyński

2021

IJMS

Self Cite

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Due to the fact that surfactant molecules are known to alter the structure (and consequently the function) of a protein, protein–surfactant interactions are very important in the biological, pharmaceutical, and cosmetic industries. Although there are numerous studies on the interactions of albumins with surfactants, the investigations are often performed at fixed environmental conditions and limited to separate surface-active agents and consequently do not present an appropriate comparison between their different types and structures. In the present paper, the interactions between selected cationic, anionic, and nonionic surfactants, namely hexadecylpyridinium chloride (CPC), hexadecyltrimethylammonium bromide (CTAB), sodium dodecyl sulfate (SDS), polyethylene glycol sorbitan monolaurate, monopalmitate, and monooleate (TWEEN 20, TWEEN 40, and TWEEN 80, respectively) with bovine serum albumin (BSA) were studied qualitatively and quantitatively in an aqueous solution (10 mM cacodylate buffer; pH 5.0 and 7.0) by steady-state fluorescence spectroscopy supported by UV spectrophotometry and CD spectroscopy. Since in the case of all studied systems, the fluorescence intensity of BSA decreased regularly and significantly under the action of the surfactants added, the fluorescence quenching mechanism was analyzed thoroughly with the use of the Stern–Volmer equation (and its modification) and attributed to the formation of BSA–surfactant complexes. The binding efficiency and mode of interactions were evaluated among others by the determination, comparison, and discussion of the values of binding (association) constants of the newly formed complexes and the corresponding thermodynamic parameters (ΔG, ΔH, ΔS). Furthermore, the influence of the structure of the chosen surfactants (charge of hydrophilic head and length of hydrophobic chain) as well as different environmental conditions (pH, temperature) on the binding mode and the strength of the interaction has been investigated and elucidated.

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Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

Cited by 7 publications

References 44 publications

Photothermal Modulation of Dynamic Covalent Poly(ethylene glycol)/PEDOT Composite Hydrogels for On-Demand Drug Delivery

Photothermal Modulation of Dynamic Covalent Poly(ethylene glycol)/PEDOT Composite Hydrogels for On-Demand Drug Delivery

Influence of Low Molecular Weight Salts on the Viscosity of Aqueous-Buffer Bovine Serum Albumin Solutions

On the Effect of pH, Temperature, and Surfactant Structure on Bovine Serum Albumin–Cationic/Anionic/Nonionic Surfactants Interactions in Cacodylate Buffer–Fluorescence Quenching Studies Supported by UV Spectrophotometry and CD Spectroscopy

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