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PubMed1965

ADSORPTION OF CATIONIC (BASIC) DYES BY FIXED YEAST CELLS.

Giles, Charles H. (The University of Strathclyde, Glasgow, Scotland), and Robert B. McKay. Adsorption of cationic (basic) dyes by fixed yeast cells. J. Bacteriol. 89:390-397. 1965.-The adsorption of 10 typical cationic dyes on formalin-fixed yeast cells has been studied by determining isotherms, and the results are consistent with an ion-exchange mechanism. The adsorption on this complex substrate is similar to that on the simpler substrate, alumina. The dyes are probably aggregated when adsorbed, and the size of the aggregates increases with increase in the molecular weight of the dye ion. After considering the possible adsorption sites, and comparing the data with adsorption on simpler substrates, we suggest that the most important adsorption sites may be phosphate or other strongly acidic groups.

Adsorption↗
PubMed1999

Bovine serum albumin adsorption on titania surfaces and its relation to wettability aspects.

The adsorption of bovine serum albumin (BSA) from sodium chloride solution and Hanks' balanced salt solution (HBSS) onto TiO2-silicon surfaces is studied by reflectometry in stagnation point flow. The results are compared with those obtained by dynamic contact-angle (DCA) analysis of titanium substrates. The adsorption isotherms show that the adsorbed amount of protein always is lower in HBSS, that is, in the presence of calcium and phosphate ions. This may be related to the increase in surface hydrophilicity caused by these ions, as suggested by the authors in previous works. The rate of adsorption also is lower in HBSS solutions. Comparison of the initial adsorption rates with the rate of mass transfer to the surface reveals that in both solvents only a small fraction of the protein that arrives at the surface adsorbs onto it. Electrostatic and/or conformational effects can explain the energy barrier to adsorption. The DCA analysis of high concentration (4 mg/mL) protein solutions shows a strong reduction of the contact-angle hysteresis, both in HBSS and in NaCl solutions, which confirms that the immediate adsorption of the protein to the surface forms a stable, hydrophilic film.

Adsorption↗
PubMed2001

Further studies on the contribution of electrostatic and hydrophobic interactions to protein adsorption on dye-ligand adsorbents.

The adsorption equilibria of bovine serum albumin (BSA), gamma-globulin, and lysozyme to three kinds of Cibacron blue 3GA (CB)-modified agarose gels, 6% agarose gel-coated steel heads (6AS), Sepharose CL-6B, and a home-made 4% agarose gel (4AB), were studied. We show that ionic strength has irregular effects on BSA adsorption to the CB-modified affinity gels by affecting the interactions between the negatively charged protein and CB as well as CB and the support matrix. At low salt concentrations, the increase in ionic strength decreases the electrostatic repulsion between negatively charged BSA and the negatively charged gel surfaces, thus resulting in the increase of BSA adsorption. This tendency depends on the pore size of the solid matrix, CB coupling density, and the net negative charges of proteins (or aqueous - phase pH value). Sepharose gel has larger average pore size, so the electrostatic repulsion-effected protein exclusion from the small gel pores is observed only for the affinity adsorbent with high CB coupling density (15.4 micromol/mL) at very low ionic strength (NaCl concentration below 0.05 M in 10 mM Tris-HCl buffer, pH 7.5). However, because CB-6AS and CB-4AB have a smaller pore size, the electrostatic exclusion effect can be found at NaCl concentrations of up to 0.2 M. The electrostatic exclusion effect is even found for CB-6AS with a CB density as low as 2.38 micromol/mL. Moreover, the electrostatic exclusion effect decreases with decreasing aqueous-phase pH due to the decrease of the net negative charges of the protein. For gamma-globulin and lysozyme with higher isoelectric points than BSA, the electrostatic exclusion effect is not observed. At higher ionic strength, protein adsorption to the CB-modified adsorbents decreases with increasing ionic strength. It is concluded that the hydrophobic interaction between CB molecules and the support matrix increases with increasing ionic strength, leading to the decrease of ligand density accessible to proteins, and then the decrease of protein adsorption. Thus, due to the hybrid effect of electrostatic and hydrophobic interactions, in most cases studied there exists a salt concentration to maximize BSA adsorption.

Adsorption↗
PubMed2003

Electrochemical optical waveguide lightmode spectroscopy (EC-OWLS): a pilot study using evanescent-field optical sensing under voltage control to monitor polycationic polymer adsorption onto indium tin oxide (ITO)-coated waveguide chips.

A new technique has been developed that combines evanescent-field optical sensing with electrochemical control of surface adsorption processes. This new technique, termed "electrochemical optical waveguide lightmode spectroscopy" (EC-OWLS), proved efficient in monitoring molecular surface adsorption and layer thickness changes of an adsorbed polymer layer examined in situ as a function of potential applied to a waveguide in a pilot study. For optical sensing, a layer of indium tin oxide (ITO) served as both a high-refractive-index waveguide and a conductive electrode. In addition, an electrochemical flow-through fluid cell was provided, which incorporated working, reference, and counter electrodes, and was compatible with the constraints of optical sensing. Poly(L-lysine)-grafted-poly(ethylene glycol) (PLL-g-PEG) served as a model, polycation adsorbate. Adsorption of PLL-g-PEG from aqueous buffer solution increased from 125 to 475 ng/cm(2 )along a sigmoidal path as a function of increasing potential between 0 and 1.5 V versus the Ag reference electrode. Upon buffer rinse, adsorption was partially reversible when a potential of >/=0.93 V was maintained on the ITO waveguide. However, reducing the applied potential back to 0 V before rinsing resulted in irreversible polymer adsorption. PLL-g-PEG modified with biotin demonstrated similar adsorption characteristics, but subsequent streptavidin binding was independent of biotin concentration. Applying positive potentials resulted in increased adsorbed mass, presumably due to polymer chain extension and reorganization in the molecular adlayer.

Adsorption↗
PubMed2005

Process modeling of in situ-adsorption of a bacterial lipase.

In situ adsorption, known as an in situ-roduct removal (ISPR) technique for low molecular mass bioproducts, was in this study applied to a bacterial exoenzyme proving that this method is also suitable for the separation of macromolecules like proteins. For this, adsorbent particles were added to growing cultures of Staphylococcus carnosus rec., therefore both production and adsorption occurred simultaneously in shaking flasks, stirred tank, or airlift bioreactor as the chosen types of fermenters. The exoenzyme lipase adsorbed rapidly and, after separating cells and adsorbents, desorbed in a packed bed column. Up to 85% of the produced lipase were recovered, fractions of these had been concentrated up to the factor 20 and purified up to a factor of 40 by the procedure. By using the airlift bioreactor an enhancement of biomass production was observed, but the necessity of the addition of an anti-foam reagent resulted in higher product losses in adsorption as well as in desorption. Production and adsorption kinetics have been modeled and applied to in situ-adsorption. The model was used to perform a parameter study in which the influence of biological and physical parameters as well as process parameters on discontinuous and continuous in situ-adsorption was investigated.

Adsorption↗
PubMed2006

Robert Boyle's chiral crystal chemistry: computational re-evaluation of enantioselective adsorption on quartz.

While searching for early examples of interactions of organic chromophores with minerals in the context of a systematic study of the process of dyeing crystals, we came across Robert Boyle's description of an experiment that may have been evidence of the enantioselective adsorption of a natural product, carminic acid (7-beta-D-glucopyranosyl-9,10-dihydro-3,5,6,8-tetrahydroxy-1-methyl-9,10-dioxo-2-anthracenecarboxylic acid), to the chiral surfaces of alpha-quartz, three centuries before such interactions became the subject of active chemical investigations. In order to determine whether Boyle did indeed observe enantioselective adsorption--albeit unbeknownst to him--we attempted to dye quartz with carminic acid according to his recipe. Quartz adsorbs carminic acid only because on heating it develops a network of microfissures that adsorb dye. This process depends on capillarity, not on specific non-covalent interactions; there is no evidence of enantioselectivity adsorption to heated crystals or enantioselective epitaxy to unheated crystals. These failures changed the focus of our inquiry: Why have almost all attempts to demonstrate the enantioselective adsorption of additives to quartz crystal surfaces been generally confounding and equivocal? In order to answer this question, we complement our experimental historical re-investigation with contemporary computational techniques for modeling crystal surface structure and the adsorption of additives. Minimizations of the energies associated with the adsorption of carminic acid to relaxed, hydrated d- and l-quartz {10(-)0} surfaces are analyzed in light of quartz's abysmal record as an enantioselective stationary phase.

Adsorption↗
PubMed2005

Modeling of the adsorption of organic compounds on polymeric nanofiltration membranes in solutions containing two compounds.

The adsorption of organic compounds in aqueous solution on polymeric nanofiltration membranes is studied; this process is one of the most important fouling mechanisms influencing the flux and retention behavior of nanofiltration membranes. It is shown that the adsorption of dissolved organic compounds on polymeric nanofiltration membranes is comparable to that on activated carbon. Freundlich and Langmuir isotherms are used to describe the relation between the adsorbed mass on the membrane and the equilibrium concentration of the organic compound in a single-compound solution. Based on these results, three models for the adsorption of solutions containing several compounds [i.e., the simple competitive adsorption model (SCAM), the model of Jain-Snoeyinck, and the model of Butler-Ockrent] were used to predict the adsorption behavior of an organic compound in an aqueous solution containing two compounds. The results of the three models were compared to experimental observations. It is shown that the SCAM allows a good prediction of the adsorption behavior.

Adsorption↗
PubMed2002

Theoretical analysis of adsorption thermodynamics for hydrophobic peptide residues on SAM surfaces of varying functionality.

At a fundamental level, protein adsorption to a synthetic surface must be strongly influenced by the interaction between the peptide residues presented by the protein's surface (primary protein structure) and the functional groups presented by the synthetic surface. In this study, semi-empirical molecular modeling was used along with experimental wetting data to theoretically approach protein adsorption at this primary structural level. Changes in enthalpy, entropy, and Gibbs free energy were calculated as a function of residue-surface separation distance for the adsorption of individual hydrophobic peptide residues (valine, leucine, phenylalanine) on alkanethiol self-assembled monolayers on gold [Au-S(CH(2))(15)-X; X = CH(3), OH, NH(3)(+), COO(-)]. The results predict that the adsorption of each type of hydrophobic residue is energetically favorable and entropy dominated on a methyl-terminated hydrophobic surface, energetically unfavorable and enthalpy dominated on a hydroxyl-terminated neutral hydrophilic surface, and very slightly favorable to unfavorable and enthalpy dominated on charged surfaces. These theoretical results provide a basis for understanding some of the fundamental effects governing protein adsorption to synthetic surfaces. This level of understanding is needed for the proactive design of surfaces to control protein adsorption and subsequent cellular response for both implant and tissue engineering applications.

Adsorption↗
PubMed1993

Thrombin and albumin adsorption to PVA and heparin-PVA hydrogels. 2: Competition and displacement.

Thrombin adsorption to polyvinyl alcohol (PVA) was different from its adsorption to polyethylene (PE)--not so much in amount, but in its affinity. Thrombin was more easily displaced from polyethylene and its adsorption was more readily prevented by prior or simultaneous exposure to albumin. From PVA (or heparin-PVA), only approximately 30% of the adsorbed protein could be removed by a series of eluents, including even harsh ones such as 2.5M NaOH and 6M guanidine; > 85% could be removed from PE. Thrombin adsorption to PVA was not affected by the presence of BSA in solution or at the surface, but was virtually prevented on PE by preexposure to or adsorption with BSA. Heparin-PVA was not much different than PVA in most of these experiments, but did exhibit a "Vroman effect". In the absence of fibrinogen or antithrombin III, there was a maximum in thrombin adsorption from plasma at a plasma concentration of 1%. The behavior on this surface was dependent on both exposure time and protein concentration. These studies highlight the complexity of the interaction between plasma proteins and polymer surfaces (particularly hydrogel surfaces) and the difficulty of obtaining a clear picture of what happens when a single protein interacts with a polymer in the presence of other proteins.

Adsorption↗
PubMed1995

Blood-biomaterial interactions in a flow system in the presence of bacteria: effect of protein adsorption.

An in vitro continuous flow system with whole human blood was used to study blood-biomaterial interactions on a base polyurethane and three modified surfaces in the presence and absence of circulating Staphylococcus epidermidis. We hypothesized that the composition of the protein layer adsorbed on the surface of the biomaterial would influence the response of blood components and bacteria. We examined the test surfaces for adsorption of nine plasma proteins and adsorption profiles differed on the four surfaces. The positively charged surface, UC, adsorbed significantly higher amounts of fibronectin (P < .01), von Willebrand factor (P < .01), and fibrinogen (P < .05) than the other materials. As a consequence of increased adsorption of these adhesive proteins, the adhesion of platelets and bacteria was greater on UC than on any other surface. On the base polyurethane, BC, and the negatively charged surface, UA, protein adsorption was low, and these materials were largely free of adherent blood cells and bacteria. The heparinized surface, UH, adsorbed higher quantities (P < .01) of Hageman factor and high molecular weight kininogen relative to the other surfaces. Platelet adhesion, and surface coagulation were prominent on UC, and may have contributed to increased bacterial adhesion on this surface. In the presence of circulating bacteria, adsorption was generally lower than in the absence of bacteria. The pattern of protein adsorption was largely unaffected by the strain of circulating bacteria, but platelet responses (adhesion and activation) were greater in the presence of slime-producing S. epidermidis as compared to the non-slime-producing strain, suggesting that slime may have a direct activating effect on platelets.

Adsorption↗
PubMed2003

Theoretical analysis of adsorption thermodynamics for charged peptide residues on SAM surfaces of varying functionality.

Cellular response to an implant is largely controlled by protein adsorption because cells directly interact with the adsorbed protein rather than the implant surface. Protein adsorption will occur when the change in Gibbs free energy (Delta G) of the system decreases during the adsorption process. Electrostatic interactions between charged peptide residues presented by a protein's surface and surface functional groups greatly contribute to the Delta G of protein adsorption. In this study, semiempirical molecular orbital calculations were used to theoretically determine the adsorption enthalpy between charged peptide residues [aspartic acid (-1), glutamic acid (-1), and arginine (+1)] and functionalized SAM surfaces [methyl, hydroxyl, amine (+1), and carboxylic acid (-1)]. Additional enthalpic and entropic contributions attributed to water restructuring effects were then approximated based on literature values for functional group solvation and considered along with the calculated enthalpy values to estimate the change in Delta G for each residue/surface system as a function of surface separation distance. The results predict long-range attraction and repulsion to the opposite and same-charge residue/surface systems, respectively, followed by strong short-range repulsion caused by functional group dehydration. Short-range repulsion alone was predicted for the charged residues on the methyl and hydroxyl surfaces. These results provide a theoretical quantitative description of fundamental mechanisms governing protein adsorption behavior and provide a basis for the development of a knowledge-based surface design approach to control biological response.

Adsorption↗
PubMed2003

Competitive plasma protein adsorption onto fluorinated polyimide surfaces.

A series of fluorinated polyimides cured at different temperatures was prepared, and plasma protein adsorption and platelet adhesion onto the polyimide films were evaluated in vitro using scanning electron microscopy, a micro-bicinchoninic acid protein assay, and a gold-colloid-labeled immunoassay. In particular, we focused on competitive plasma protein adsorption onto polyimide film because elucidation of the competitive adsorption mechanism is needed for a good understanding of in vivo biocompatibility of polyimide. Interestingly, the trend of IgG adsorption onto the polyimide surface measured in human plasma was completely contrary to that observed with IgG dissolved in PBS, and the adsorption increased with an increase in the curing temperature. We propose that the human plasma F(c) region in IgG might selectively adsorb onto polyimide film cured at high temperatures because of competitive plasma protein adsorption to the surface.

Adsorption↗
PubMed2007

Quantification of fibrinogen adsorption onto 316L stainless steel.

Adsorption of the plasma protein fibrinogen (Fb) onto 316L stainless steel (316L SS) was observed and quantified using both in situ and ex situ atomic force microscopy techniques. Industry standard mechanical and electrochemical polishing techniques were used to prepare bulk alloy 316L SS samples, rendering the surfaces flat enough to directly observe and measure Fb adsorption. The data were analyzed kinetically using a Langmuir model. Largely irreversible adsorption was found on the 316L SS surface with an adsorption rate constant (k(o)) of 1.9 x 10(-4) mL microg(-1) s(-1) using the ex situ method and 1.7 x 10(-4) mL microg(-1) s(-1) using the in situ method. Additionally, protein conformation and assembly orientation on these surfaces were documented, where the adsorption pattern appeared random. Complete area coverage was never obtained. That is, after adsorption for over 5 time constants (5tau), voids in the structure were always observed.

Adsorption↗
PubMed2007

Protein adsorption and zeta potentials of a biphasic calcium phosphate ceramic under various conditions.

An investigation on the relationship between protein adsorption and zeta potentials of a biphasic calcium phosphate (BCP) ceramic was carried out. Zeta potentials of the BCP ceramic particles were measured at various aqueous solutions. Bovine serum album (BSA) and its competitive adsorption with lysozyme (LSZ) on BCP were investigated using conventional protein adsorption and polyacrylamide gel electrophoresis (PAGE) methods. The results showed that zeta potential and the amount of adsorbed BSA were both influenced by pH, ionic strength, Ca2+ and PO4(3-) concentrations in the buffers. The variation tendencies of BSA adsorption were consistent with that of zeta potentials to some extent. The co-adsorption of BSA and LSZ on BCP was confirmed by the PAGE gel pattern. The semi-quantitative analysis for the detected protein bands proved that LSZ had higher affinity for BCP than BSA and would preferentially bind to the surface. Electrostatic interaction played an important role in protein adsorption on the surface of the BCP ceramic particles.

Adsorption↗
PubMed1976

Kinetics of interfacial ATP adsorption and anionic exchange with a synaptic membrane protein.

A study was conducted on the adsorption of 14C-ATP to a surface film of a hydrophobic protein derived from synaptic membranes isolated from bovine cerebellum. The adsorption of ATP to the protein film followed a rate law based on diffusion and an energy barrier to adsorption, the rate law being generally applicable to the adsorption of ions to a charged interface. Studies were also carried out on the displacement of ATP from the film by the injection of other nucleotides, inorganic phosphates, and other anions. The kinetics conformed to a rate law based on diffusion and displacement. The most important factor in the displacement of ATP was the magnitude of charge of the anion, while steric factors were relatively minor. However, from a consideration of the energy barrier to adsorption it appeared that steric factors play a greater role in the adsorption of ATP. The results are discussed in relationship to the configurational aspects of the surface film as well as their possible significance in synaptic function.

Adenosine Triphosphate↗
PubMed2002

Aspects on the interaction between sodium carboxymethylcellulose and calcium carbonate and the relationship to specific site adsorption.

The mechanisms of adsorption and association for sodium carboxymethylcellulose (NaCMC) in calcium carbonate suspensions have been determined from isothermal calorimetry and adsorption measurements. The equilibrium adsorption isotherms were determined by two different methods of separation; a depletion method and a serum exchange method. The enthalpy of dilution for NaCMC was determined on supernatants obtained from the calcium carbonate suspensions in order to investigate the interaction between NaCMC and dissolved species from the mineral. For comparison, NaCMC was injected into CaCl(2) solutions in order to determine the role of calcium ions in the adsorption process. The initial part of the adsorption isotherm showed a quasi-infinite slope indicating a high affinity for the NaCMC to the calcium carbonate surface, which was significantly reduced when anionic sodium polyacrylate was preadsorbed onto the calcium carbonate implying competitive adsorption. An endothermic enthalpy change was observed between the NaCMC and the calcium carbonate surface, suggesting attachment of the carboxylic acid groups onto the hydrated calcium sites. A similar endothermic enthalpy was observed when NaCMC was injected into CaCl(2) solutions or supernatants obtained from the calcium carbonate suspensions, indicating a complexation of carboxylic acid groups and hydrated calcium ions. It was concluded that the mechanisms of interaction of NaCMC in calcium carbonate suspensions are primarily an association between NaCMC and Lewis acid sites on the calcium carbonate surface and the formation of NaCMC-Ca(2+) complexes in the bulk solution, both of which will be affected by the amount of anionic sodium polyacrylate present.

Adsorption↗
PubMed2002

Concentration effects on adsorption of bacteriophage T4 lysozyme stability variants to silica.

The adsorption kinetics and dodeceyltrimethylammonium bromide-mediated elution of the wild type and two structural stability mutants of bacteriophage T4 lysozyme were recorded in situ, at silica surfaces. Experiments were performed at different solution concentrations, ranging from 0.01 to 1.0 mg/ml. Plateau values of adsorbed mass generally increased with increasing solution concentration, with the adsorbed layer being only partially eluted by buffer. Treatment with surfactant removed more of the adsorbed protein in each case, with the remaining adsorbed mass varying little with concentration. Comparison of the data to an adsorption mechanism allowing for three adsorbed states, distinguished by binding strength, showed that the fraction of adsorbed molecules present in the most tightly bound state (state 3) decreased as adsorption occurred from solutions of increasing concentration. However, the absolute amounts of state 3 molecules present in each case were less dependent on solution concentration. Adsorption of T4 lysozyme into state 3 is suggested to occur early in the adsorption process and continue until some critical surface concentration is reached. Beyond this critical value of adsorbed mass, adsorption is suggested to progress with adoption of more loosely bound states.

Adsorption↗
PubMed2002

Effects of acetonitrile on adsorption behavior of bovine serum albumin onto synthetic calcium hydroxyapatite particles.

The objective of this study was to examine the effects of acetonitrile (AN) on the adsorption behavior of bovine serum albumin (BSA) onto calcium hydroxyapatite [Ca10(PO4)6(OH)2 Ca10, Hap] materials by combining the ultraviolet (UV) and circular dichroism (CD) measurements of BSA solution. The structural change of BSA molecules with addition of AN was investigated by UV and CD spectroscopy measurements prior to studying adsorption behavior of BSA onto Hap. The CD spectra revealed that the fraction of alpha-helical content of BSA is remarkably decreased at AN concentrations above 30 vol.%, while beta-sheet content is increased. On the other hand, the percentages of random coil and turn contents were decreased only slightly. In addition to this secondary structural change of BSA, the UV spectra suggested that the tertiary structure of protein molecules was also changed by the addition of large amounts of AN; BSA molecules associate to form molecular aggregates at [AN]> or =40 vol.%. From the adsorption of BSA onto Hap particles (ca. 30 nm in the particle length) from a water-AN mixed solution, it was revealed that the adsorption behavior of BSA strongly depends on the change of secondary and tertiary structures of BSA by addition of AN. The contraction of BSA molecules at low AN concentrations (10-20 vol.%) gave their small cross-sectional area, providing a large amount of adsorption (n(BSA)), although n(BSA) was decreased above 30 vol.% AN by enlargement of BSA molecules with solvation and unfolding some alpha-helix domains. The n(BSA) values of the systems with AN exhibited a maximum; n(BSA) was increased at a lower BSA concentration region, although it was decreased at a higher BSA concentration due to self-association. Accompanying the change of n(BSA) with AN addition, the maxima of electrophoretic mobility (em) of the Hap particles were observed for the systems with AN, although the em of Hap particles was normally increased and saturated with increase in protein coverage for the native structure on the system without AN. On the other hand, because the aggregated BSA molecules could be cooperatively bound, the adsorption of BSA onto the Hap particles with large size (108 nm in the particle length) was enhanced in the presence of AN.

Acetonitriles↗