Abstract:This work shows buffer choice and buffer concentration can drastically affect protein adsorption. We used ATR/FTIR to compare the adsorption kinetics and secondary structural evolution of BSA, IgG, fibrinogen and lysozyme on a Ge surface, buffered in phosphate buffered saline (PBS) and tris(hydroxymethyl)aminomethane hydrochloride (Tris-HCl) at pH 7.4. The adsorption behaviors of the four proteins are multilayer in nature, and all exhibit a short period of rapid initial adsorption with larger secondary structu… Show more
“…Thus, studies evaluating adsorption dependent on the solvent have been described by the batch method to clarify Ab adsorption on HAp in phosphate-buffered saline, 37 Ab adsorption on silica-titania hybrids in phosphate-buffered saline and 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid, 38 and Ab, IgG, Fgn and lysozyme adsorptions on germanium in phosphate-buffered saline or Tris-HCl. 39 The conformations of the Ab adlayer on gold 40 and the Fn adlayer on HAp 41 involving the binding of a monoclonal antibody have also been discussed.…”
When biomaterials are implanted into an animal body, the body fluid proteins initially adsorb and then cells recognize these surfaces. Adherent cell functions respond differently to diverse biomaterial surfaces with different properties. Thus, an understanding of cellular responses to biomaterials is crucial for effective control of biomaterial − cell interactions. I have researched how to clarify interfacial phenomena via protein adsorption and subsequent cell adhesion to hydroxyapatite nanocrystals using a quartz crystal microbalance with a dissipation technique. In this review, I focused on the current understanding of enhanced biocompatibility by exploring the roles of protein mediation at the interface. The most promising nano-bio interfaces are explained, and different protein adsorption and cell adhesion processes are highlighted depending on their interfacial states. This approach will clarify several ambiguities of interfacial phenomena between biomaterials and cells and will help in the design of novel biomaterials that can be implanted.
“…Thus, studies evaluating adsorption dependent on the solvent have been described by the batch method to clarify Ab adsorption on HAp in phosphate-buffered saline, 37 Ab adsorption on silica-titania hybrids in phosphate-buffered saline and 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid, 38 and Ab, IgG, Fgn and lysozyme adsorptions on germanium in phosphate-buffered saline or Tris-HCl. 39 The conformations of the Ab adlayer on gold 40 and the Fn adlayer on HAp 41 involving the binding of a monoclonal antibody have also been discussed.…”
When biomaterials are implanted into an animal body, the body fluid proteins initially adsorb and then cells recognize these surfaces. Adherent cell functions respond differently to diverse biomaterial surfaces with different properties. Thus, an understanding of cellular responses to biomaterials is crucial for effective control of biomaterial − cell interactions. I have researched how to clarify interfacial phenomena via protein adsorption and subsequent cell adhesion to hydroxyapatite nanocrystals using a quartz crystal microbalance with a dissipation technique. In this review, I focused on the current understanding of enhanced biocompatibility by exploring the roles of protein mediation at the interface. The most promising nano-bio interfaces are explained, and different protein adsorption and cell adhesion processes are highlighted depending on their interfacial states. This approach will clarify several ambiguities of interfacial phenomena between biomaterials and cells and will help in the design of novel biomaterials that can be implanted.
“…2 Upon β-gal adsorption protein-specific amide bands at 1645 (amide I) and 1545 cm −1 (amide II) appear in the IR spectrum, the intensities of which remain constant after removal of the protein solution and extensive washing with pure H 2 O. However, washing the film with Na 2 HPO 4 solutions of increasing concentration clearly depletes the intensities of the protein-specific bands and generates a new band at 1080 cm −1 characteristic of [36]. Buffer induced protein desorption was also observed when using HEPES (4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid) instead of McIlvaine’s buffer (not shown).Fig.…”
BackgroundActivity retention upon enzyme adsorption on inorganic nanostructures depends on different system parameters such as structure and composition of the support, composition of the medium as well as enzyme loading. Qualitative and quantitative characterization work, which aims at an elucidation of the microscopic details governing enzymatic activity, requires well-defined model systems.ResultsVapor phase-grown and thermally processed anatase TiO2 nanoparticle powders were transformed into aqueous particle dispersions and characterized by dynamic light scattering and laser Doppler electrophoresis. Addition of β-galactosidase (β-gal) to these dispersions leads to complete enzyme adsorption and the generation of β-gal/TiO2 heteroaggregates. For low enzyme loadings (~4% of the theoretical monolayer coverage) we observed a dramatic activity loss in enzymatic activity by a factor of 60–100 in comparison to that of the free enzyme in solution. Parallel ATR-IR-spectroscopic characterization of β-gal/TiO2 heteroaggregates reveals an adsorption-induced decrease of the β-sheet content and the formation of random structures leading to the deterioration of the active site.ConclusionsThe study underlines that robust qualitative and quantitative statements about enzyme adsorption and activity retention require the use of model systems such as anatase TiO2 nanoparticle agglomerates featuring well-defined structural and compositional properties.Electronic supplementary materialThe online version of this article (doi:10.1186/s12951-017-0283-4) contains supplementary material, which is available to authorized users.
“…In addition, the TMBD-DIEN solution contains a high concentration of phosphate anions that are expected to strongly interact with the positively charged proteins. The formation of strong complexes between phosphate ions and proteins has been largely documented in literature [34] and already associated with the explanation of changes in the migration behavior of proteins in CZE [29,[35][36][37].…”
This paper reports the results of a study performed to investigate the dependence of the performance of protein separation by capillary zone electrophoresis (CZE) on the anionic component of the electrolyte solutions consisting of 20 mM N,N,N 0 ,N 0 -tetramethyl-1,3-butanediamine (TMBD) titrated to either pH 4.0 or pH 6.5 with either a monoprotic or a polyprotic acid. With the exception of hydrochloric acid, the acids were selected among those commonly used as the constituents of the solutions employed for protein analysis by either HPLC or CZE. TMBD was chosen for its effectiveness at preventing the interactions of proteins with the inner wall of bare fusedsilica capillaries. The performance of separations was evaluated using four basic model proteins having pI value and molecular mass ranging from 9.5 to 11.0 and from 12,400 to 25,000 Da, respectively. It is shown that the different acids used as the components of the background electrolyte solutions, all containing the same concentration of TMBD, affect to different extents both migration time and peak shape of the tested proteins. The performance displayed by the BGE containing phosphate ions is enhanced using TMBD in combination with diethylenetriamine, an aliphatic vicinal triamine having effective buffering capacity at pH 4.0 and capability at minimizing protein-capillary wall interactions. The reported experimental evidences are discussed based on the possible interactions that the phosphate ions are known to establish with both the protein molecules and the surface of bare fused-silica capillaries.
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