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Biomedical subjects

B D Ratner

Publications and source records attributed to B D Ratner.

At least 55 records · Page 3Linked to original sources
PubMed1993

Variations between Biomer lots. 2: The effect of differences between lots on in vitro enzymatic and oxidative degradation of a commercial polyurethane.

In vitro degradation of two lots of Biomer, a commercial poly(ether urethane urea), has been investigated in order to understand possible mechanisms for in vivo degradation. Two lots of Biomer, BSUA001 and BSP067, were used in the study. Lot BSUA001 contained a poly(diisopropylaminoethyl-methacrylate), an ultraviolet-stabilizing additive. This additive was absent in lot BSP067. Samples of each lot were exposed to two hydrolytic enzymes, papain and leucine aminopeptidase, and to hydrogen peroxide for 24 h. The extent of degradation was assessed using high-pressure gel permeation chromatography and x-ray photoelectron spectroscopy (XPS). Statistically significant changes in the molecular-weight distribution occurred in lot BSP067 for all three treatments. Only the hydrogen peroxide treatment resulted in statistically significant changes in the molecular weight of lot BSUA001. XPS data for samples of lot BSUA001 that had been treated with hydrogen peroxide revealed the formation of nitroso groups and protonated amines at the surface. The data suggest that surface chemistry is important for enzyme catalyzed degradation, while permeability is important for degradation by hydrogen peroxide.

Biocompatible Materials↗
PubMed1993

Effect of polyol type on the surface structure of sulfonate-containing polyurethanes.

Polyurethanes based upon polytetramethylene oxide (PTMO) as the polyol and derivatized with propyl sulfonate functionality pendant from the urethane nitrogen have previously been shown to possess good blood-contacting properties. Other investigators have shown that sulfonated polyurethanes containing polyethylene oxide (PEO) as the soft segment are much more thrombogenic than those containing PTMO as the soft segment. In this article, the surface properties of sulfonated polyurethanes based upon either PTMO or PEO are compared. Dynamic contact angle measurements show a significant decrease in the receding angles of the sulfonated PTMO-containing polyurethane as compared to its nonsulfonated precursor polymer. No significant difference is seen between the receding contact angles of either the sulfonated PEO-based polyurethane or its nonsulfonated analog. Variable-angle electron spectroscopy for chemical analysis (ESCA) studies of sulfonated PTMO-based polyurethane performed at room temperature show that there is a significant decrease in sulfur content at the surface. In contrast, the sulfonated PEO-based polyurethane showed little change in sulfur content with take-off angle. Finally, ESCA studies of freeze-dried surfaces show a significant increase in sulfur near the surface of the sulfonated PTMO-based polymer as compared to vacuum-dried samples but show no such increase for the sulfonated PEO-based polyurethane. It is suggested that the ability of the sulfonate functionality to be expressed at the surface may explain the observed differences in blood compatibility between the sulfonated polyurethanes based upon polyols of varying hydrophilicity.

Absorption↗
PubMed1993

New ideas in biomaterials science--a path to engineered biomaterials.

Our existing biomaterials, although demonstrating generally satisfactory clinical performance, were developed based upon a trial-and-error optimization approach rather than being engineered to produce the desired interfacial reaction. Most biomaterials exhibit a nonspecific biological reaction, with sluggish kinetics and a broad spectrum of active processes simultaneously occurring. This article describes materials science nanotechnology, and molecular biology techniques that may permit the synthesis of precisely engineered surfaces. Such surfaces might demonstrate rapid, precise reactions with proteins and cells. This opens the question, "what type of specific surface bioreactions do we want?" New thoughts on biocompatibility are presented that may be helpful in the design of specific surfaces yielding precise, defined biological responses.

Biocompatible Materials↗
PubMed1993

In vitro platelet interactions in whole human blood exposed to biomaterial surfaces: insights on blood compatibility.

A short-term in vitro test to study platelet interactions with biomaterials is described. Using fresh human blood and a modified Chandler loop system, beta-thromboglobulin release was measured. Also, adherent platelets were observed by using scanning electron microscopy (SEM) and a colorimetric stain specific for human platelet GPIIIa. Materials studied in these experiments were polyethylene (PE), Biomer, poly(vinyl alcohol) (PVA), and a polyurethane prepared with octadecyl pendant groups (ODCE). Four blood reactions were observed: (1) Platelets continually adhere and activate on the Biomer; (2) platelets initially adhere and activate but then spread to a thin, passivating film on the PE; (3) platelets do not adhere to the PVA surface but continually react with it upon contact; and (4) platelets neither adhere to nor activate on the ODCE surface. Reactions (2) and (4) are considered characteristic of blood-compatible materials.

Biocompatible Materials↗
PubMed1993

ESCA surface characterization of four IUPAC reference polymers.

Four reference polymers studied by the International Union of Pure and Applied Chemistry working party on interactions of polymers with living systems were characterized by electron spectroscopy for chemical analysis. The surface of a polyethylene specimen was found to consist of only hydrocarbon (-CH2-) groups, as expected. Similarly, the surface of a poly(dimethyl siloxane) was found to be in close agreement with the expected stoichiometry of this polymer. The surface of the PVC sample showed a high surface concentration of hydrocarbon-rich plasticizer. Also, Si, O and Zn were detected. Cellulose coil specimens were heavily silicone contaminated. A 24 h rinse of this material in water reduced the Si level to 5%, and produced a surface spectrum closer to that expected for cellulose.

Cellulose↗
PubMed1993

Analysis of biomedical polymer surfaces: polyurethanes and plasma-deposited thin films.

The surface characterization of biomaterials is important for understanding the biological reactivity of surfaces and for monitoring surface reproducibility and contamination. Electron spectroscopy for chemical analysis (ESCA), secondary ion mass spectrometry (SIMS), contact-angle methods, vibrational spectroscopic methods, and scanning probe microscopies are briefly reviewed. Examples are presented using these methods to characterize RF plasma-deposited surfaces based upon acetone and oxygen for cell culture and Biomer¿ surfaces.

Biocompatible Materials↗
PubMed1993

Surface properties of RGD-peptide grafted polyurethane block copolymers: variable take-off angle and cold-stage ESCA studies.

Variable take-off angle and cold-stage ESCA measurements were utilized to analyze the surface composition of five polyurethane block copolymers. The polymers studied included a PTMO-polyurethane control, a carboxylated version of the control polyurethane, and three different peptide grafted (GRGESY, GRGDSY, and GRGDVY) polyurethanes. On dry samples the nitrogen signal detected using ESCA decreased with increasing take-off angle (i.e. as the specimen was probed closer to the surface) for all five polymers. This was believed to be due to the depletion of nitrogen-containing urethane hard segments at the surface. For all five polymers, the surface nitrogen concentration, associated with the hard segment, increased upon hydration. A greater increase of nitrogen concentration was observed for the peptide grafted polymers which suggests that grafting of the hydrophilic peptides to the polyurethane augments the hard segment enrichment at the surface upon hydration. Upon dehydration, the nitrogen concentration decreased for all five polymers suggesting migration of the more hydrophobic PTMO soft segment to the surface. In vitro endothelial cell adhesion showed an increase of cell attachment on prehydrated RGD-containing peptide grafted polyurethanes, but not on the other polymers. This result suggests an enhancement of peptide density at the aqueous interface, in good agreement with the ESCA studies.

Amino Acid Sequence↗
PubMed1993

Surface analysis of hydrogel contact lenses by ESCA.

We used electron spectroscopy for chemical analysis (ESCA) to examine the surface chemistry of polymacon, tefilcon, and bufilcon hydrogel contact lenses. Worn and unworn water-cleaned and surfactant-cleaned lenses were compared. The surface chemistry of unworn lenses, which were used as controls, consisted of approximately 70% carbon, 25% oxygen, and < 10% other elements (i.e., silicon, sulfur, sodium, nitrogen, and zinc). In general, surfactant cleaning removed silicon contamination, but left a residue containing sulfur and zinc. The increase in the nitrogen/carbon (N/C) ratio for worn bufilcon and polymacon lenses was significantly greater than the N/C ratio for unworn bufilcon and polymacon lenses. As a group the worn ionic lenses (bufilcon) showed a greater N/C ratio than the worn nonionic lenses (polymacon, tefilcon). The nitrogen that appears on all worn lenses probably represents adherent as well as adsorbed surface proteins. The highest N/C ratios were found on a pair of pathologically deposited lenses and on the lens with the longest wearing time (2 years). For the bufilcon and polymacon lenses, the differences observed in the ESCA data for the unworn and worn lenses suggest that contact lenses begin interacting with the tear film within 1 minute (the shortest wearing time in this study).

Cations↗
PubMed1992

Variations between Biomer lots. I. Significant differences in the surface chemistry of two lots of a commercial poly(ether urethane).

We have studied the surface chemistry of two lots of Biomer (BSP067 and BSUA001), a widely used commercial poly(ether urethane) (PEU). Although transmission infrared adsorption studies revealed no differences in the bulk chemistry of the two lots, the surface chemistry, as seen by x-ray photoelectron spectroscopy (XPS) and static secondary ion mass spectrometry (SIMS), was different. Lot BSP067 showed soft-segment enrichment at the surface, which is typical of PEU. Lot BSUA001 showed no evidence of either hard- or soft-segment PEU components at the surface. The surface of this lot was completely covered with a nonextractable additive identified as poly(diisopropyl amino ethyl methacrylate). Small amounts of a low-molecular-weight antioxidant were observed at the surface of both samples. Because the biological response to polymers is dependent on surface structure, these results are of considerable importance to biomaterials research.

Antioxidants↗
PubMed1992

Glow discharge plasma deposition of tetraethylene glycol dimethyl ether for fouling-resistant biomaterial surfaces.

The glow discharge plasma deposition (GDPD) of tetraethylene glycol dimethyl ether is introduced as a novel method for obtaining surfaces that are resistant to protein adsorption and cellular attachment. Analysis of films by x-ray photoelectron spectroscopy and several biological assays indicate the formation of a fouling-resistant, PEO-like surface on several substrata (e.g., glass, polytetrafluoroethylene, polyethylene). Adsorption of 125I-radiolabelled proteins (fibrinogen, albumin and IgG) from buffer and plasma was very low (typically less than 20 ng/cm2) when compared to the untreated substrata, which exhibited much higher levels of protein adsorption. Not all coated substrata adsorbed equal amounts of protein (e.g., coated glass samples typically adsorbed more protein than coated polyethylene or coated polytetrafluoroethylene samples), suggesting that the substratum used may affect the amount of protein adsorbed. Measurement of dynamic platelet adhesion, using epifluorescent video microscopy, and endothelial cell attachment further demonstrates the short-term nonadhesiveness of these surfaces.

Adsorption↗
PubMed1992

Postadsorptive transitions in fibrinogen adsorbed to polyurethanes: changes in antibody binding and sodium dodecyl sulfate elutability.

Residence time-dependent changes in fibrinogen after adsorption to six different polyurethanes were examined by measuring polyclonal antifibrinogen binding to the adsorbed protein. The amount of adsorbed fibrinogen that could be eluted by sodium dodecyl sulfate (SDS) was also measured. Baboon fibrinogen was first adsorbed from dilute plasma to the polymers, which were then stored in either buffer or buffered albumin solution prior to testing. Subsequently, the amount of antifibrinogen bound by the adsorbed fibrinogen was measured using a direct enzyme linked immunosorbent assay (ELISA). Alternatively, the surface with the adsorbed fibrinogen was soaked in a 3% SDS solution, and the amount of retained 125I-radiolabeled fibrinogen was measured. With increasing residence time, decreases in both antibody binding and the SDS elutability of the adsorbed fibrinogen occurred, but the rate of change was dependent on the polyurethane to which the fibrinogen was adsorbed. In addition, the antibody binding per unit of adsorbed fibrinogen, when measured immediately after the adsorption step, varied by approximately a factor of 3 among the various polyurethanes. When the protein-coated surfaces were stored in buffered albumin solution rather than buffer, the decrease in the reactivity of fibrinogen with residence time did not occur on some of the surfaces. This study shows that the chemical properties of the adsorbing surface influence the rate at which adsorbed fibrinogen undergoes change. The significance of the polymer-dependent changes in adsorbed fibrinogen with respect to blood reactions with polymers is discussed.

Adsorption↗
PubMed1992

Adsorption of baboon fibrinogen and the adhesion of platelets to a thin film polymer deposited by radio-frequency glow discharge of allylamine.

Platelet adhesion under static and flow conditions from a washed platelet suspension containing albumin to a polymer deposited by radio-frequency glow discharge of allylamine vapour on a poly(ethylene terephthalate) substrate was measured. Electron spectroscopy for chemical analysis was used to characterize the surface. Fibrinogen adsorption from a series of dilute plasma solutions to radio-frequency glow discharge/allylamine, measured using 125I radiolabelled baboon fibrinogen, increased with decreasing plasma dilution to a level much higher than that previously observed on polyurethanes. Elutability by sodium dodecyl sulphate of fibrinogen adsorbed from dilute plasma also increased with increasing plasma concentration, but fibrinogen preadsorbed from plasma became non-elutable when surfaces were stored in buffer for 5 d before contact with sodium dodecyl sulphate. Platelet adhesion to substrates which had been pre-adsorbed with dilute plasma was measured using baboon platelets radiolabelled with 111In. Adhesion greatly decreased as the plasma concentration used for preadsorption increased, suggesting that non-specific platelet binding to the bare surface occurs when protein coverage is incomplete. Non-specific platelet binding was inhibited to varying degrees by preadsorption of different proteins to the surface. Platelet adhesion to surfaces preadsorbed with dilute (1.0%) baboon and human plasmas lacking fibrinogen (i.e. serum, heat-defibrinogenated plasma and congenitally afibrinogenemic plasma) was diminished compared with normal plasma. Addition of exogenous fibrinogen to the deficient plasma partially restored platelet adhesion to normal levels. Adhesion to surfaces preadsorbed with human plasma deficient in von Willebrand factor was comparable to that observed with normal plasma. The plasma preadsorption studies with fibrinogen deficient media suggested that adsorbed fibrinogen is necessary for platelet adhesion to the radio-frequency glow discharge/allylamine substrate at high protein coverage. However, since adhesion was greatly reduced when the plasma preadsorbed substrate was stored in buffer before platelet contact, the conformation of adsorbed fibrinogen is also important in mediating platelet adhesion to radio-frequency glow discharge.

Adsorption↗
PubMed1992

Surface characterization of 2-hydroxyethyl methacrylate/styrene copolymers by angle-dependent X-ray photoelectron spectroscopy and static secondary ion mass spectrometry.

The surface composition and structure of three structurally distinct amphiphilic copolymers of 2-hydroxyethyl methacrylate (HEMA) and styrene have been examined with angle-dependent X-ray photoelectron spectroscopy (XPS) and static secondary ion mass spectrometry (SIMS). The phase-separated block copolymer made by anionic living polymerization, HSH-A50, showed significant surface enrichment of styrene. The outermost 2-3 A appeared to be approximately 100% styrene, with the styrene concentration decreasing to its bulk value at a depth of approximately 50 A from the surface. However, HEMA was detected in the outer 20 A of this copolymer. The presence of HEMA in the surface region implies this copolymer may undergo significant restructuring when hydrated in a hydrophilic environment (as opposed to the hydrophobic environment in which the sample was prepared and analyzed). The phase-separated block copolymer made by telechelic coupling of free radical polymerized functionalized oligomers, HSH-B60, showed only slight styrene enrichment at the surface. Both HEMA and styrene were detected at all sampling depths, including the outermost surface layer, consistent with the presence of discrete HEMA and styrene domains at the copolymer surface. Since both components are already present at the surface under hydrophobic conditions, the degree of restructuring this copolymer may undergo upon hydration should be minor. The random HEMA--styrene copolymer made by conventional free radical initiation techniques, HS-RAN50, had a surface composition that was similar to the bulk composition and independent of depth, as expected for a homogeneously mixed copolymer film.

Biocompatible Materials↗
PubMed1992

Plasma deposition for biomedical applications: a brief review.

Radio frequency plasma-deposited thin films offer an advantageous mechanism to alter the surface properties of biomaterials and medical devices without affecting the mechanical properties or primary fabrication. Such coatings are tightly adherent, conformal, and easily applied. They also exhibit excellent biocompatibility qualities. Examples are presented of four different thin film plasma treatments that show promise for reducing the platelet reactivity of materials, enhancing their ability to grow cells, preventing protein pickup by surfaces, and improving the biocompatibility of ophthalmic devices.

Adsorption↗
PubMed1991

Static secondary-ion mass spectrometric investigation of the surface structure of organic plasma-deposited films prepared from stable-isotope-labeled precursors. 1. Carbonyl precursors.

Stable-isotope-labeled carbonyl precursors (acetaldehyde, acetone, and 2-butanone) were used to create plasma-deposited films (PDFs), which were then examined by positive- and negative-ion static SIMS. This allowed hydrocarbon (HC) fragments to be distinguished from oxygen-containing fragments in the static SIMS spectra of these PDFs. Both the positive- and negative-ion static SIMS fragmentation patterns of conventional HC and oxygen-containing polymers were qualitatively examined in order to assign structural units on the PDF surface that could account for the sallent features in the static SIMS fragmentation patterns of these PDFs.

Hydrocarbons↗
PubMed1991

Baboon fibrinogen adsorption and platelet adhesion to polymeric materials.

The role of fibrinogen in mediating platelet adhesion to polymers exposed to blood plasma was studied by comparison of the effect of plasma dilution on fibrinogen adsorption and platelet adhesion, and by the use of coagulation factor deficient plasmas. Polyetherurethane substrates were first preadsorbed with dilute plasma, then contacted with washed platelets suspended in a modified, apyrase containing Tyrode's buffer. Platelet adhesion was studied under static conditions in Multiwell dishes, and also under shearing conditions using a parallel plate perfusion chamber. Fibrinogen adsorption and platelet adhesion were measured using 125I radiolabeled baboon fibrinogen and 111In radiolabeled baboon platelets, respectively. Surfaces were characterized by electron spectroscopy for chemical analysis (ESCA). When fibrinogen adsorption to Biomer was measured after 2 h contact with a series of dilute plasma solutions under static conditions, a peak in adsorption was observed from 0.26% plasma, i.e., adsorption was greater from 0.26% plasma than from either more or less dilute plasma. A peak in subsequent platelet adhesion to the plasma preadsorbed surfaces, measured after 2 h static incubation with washed platelets, was also observed but occurred on Biomer preadsorbed with 1.0% plasma. When fibrinogen adsorption was measured after 5 min contact under shearing conditions, the fibrinogen adsorption peak occurred on surfaces that had been exposed to 1.0% plasma. A peak in platelet adhesion to these preadsorbed surfaces, measured after 5 min contact with the platelet suspensions under shearing conditions, was observed on Biomer preadsorbed with 0.1% plasma. Shifts between the positions of the peaks in protein adsorption and platelet adhesion occurred on other polymers tested as well. Platelet adhesion was almost completely inhibited when baboon and human plasmas lacking fibrinogen (i.e., serum, heat defibrinogenated plasma, and congenitally afibrinogenemic plasma) were used. Platelet adhesion was restored to near normal when exogenous fibrinogen was added to fibrinogen deficient plasmas. Adhesion was also inhibited completely when a monoclonal antibody directed against the glycoprotein IIb/IIIa complex was added to the platelet suspension. Platelet adhesion to surfaces preadsorbed to von Willebrand factor deficient plasma was the same as to surfaces preadsorbed with normal plasma. While it appears that surface bound fibrinogen does mediate the initial attachment of platelets to Biomer, the observation that the fibrinogen adsorption and platelet adhesion maxima do not coincide exactly also suggests that the degree of subsequent platelet adhesion is dictated not only by the amount of surface bound fibrinogen but also by its conformation.

Adsorption↗
PubMed1991

Postadsorptive transitions in fibrinogen adsorbed to biomer: changes in baboon platelet adhesion, antibody binding, and sodium dodecyl sulfate elutability.

Residence-time-dependent changes in fibrinogen after its adsorption to Biomer were examined by measuring platelet adhesion and antibody binding to the adsorbed protein, and the amount of adsorbed fibrinogen which could be eluted by sodium dodecyl sulfate (SDS). Baboon fibrinogen was first adsorbed (from either pure solution or dilute plasma) to Biomer, which was then stored in either buffer or buffered albumin solution prior to testing. Subsequently, the adherent protein layer was either probed for fibrinogen capable of mediating platelet adhesion using 111In radiolabeled, washed platelet suspensions under both static and shearing conditions, or for fibrinogen capable of binding antibody using a direct enzyme linked immunosorbent assay (ELISA). Alternatively, the surface with the adsorbed protein layer was soaked in a 3% SDS solution, and the amount of 125I radiolabeled fibrinogen retained was measured. Decreases in platelet and antibody binding, and in the SDS elutability of the adsorbed fibrinogen after it was stored in buffer were detected, although different rates of decrease were observed for each method. When the protein-coated surfaces were stored in buffered albumin solution rather than buffer, the decrease in the reactivity of fibrinogen was prevented. While each of the three assays measures a different property of adsorbed fibrinogen, this study suggests that the adherent protein undergoes time dependent conformational changes which render it less reactive toward platelets and antibodies, and more resistant to elution by SDS.

Adsorption↗