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PubMed1999

Characterization of the fibre-matrix interfacial structure in carbon fibre-reinforced polycarbosilane-derived SiC matrix composites using STEM/EELS

This paper presents a characterization study of the microstructural evolution of various carbon fibre-reinforced polycarbosilane (PCS)-derived SiC matrix composites during high temperature heat treatment. Both surface-treated and untreated carbon fibre reinforcements were investigated. The STEM/EELS technique was found to be a particularly useful characterization tool. The results of quantitative EELS linescans have been interpreted in terms of the migration of gaseous SiO and CO, produced by the reaction between the small amount of SiO2 and excess carbon within the PCS-derived SiC matrix, from the central matrix region towards the fibre-matrix interfaces. Generally, the migration of gaseous SiO and CO results in an enrichment of SiO2 at the region adjacent to the fibre-matrix interface. However, differing final composite microstructures are formed depending on the strength of the fibre-matrix bonding. In the case of strong fibre-matrix interfacial bonding where few escape channels are present, a distinct Si-C-O layer was identified within the matrix adjacent to the fibre-matrix interface; both crystalline beta-SiC and the segregated Si-O-C phase coexist in this microstructure up to at least 1450 degrees C. In the case of weak fibre-matrix bonding this oxygen segregated interfacial layer is eventually removed at high enough temperatures. The final interfacial microstructure has important consequences for the mechanical properties of the composite material.

Journal Article↗
PubMed1999

Dynamic interfacial rheology as a tool for the characterization of whey protein isolates gelation at the oil-water interface.

Heat-induced interfacial aggregation of a whey protein isolate (WPI), previously adsorbed at the oil-water interface, was studied by interfacial dynamic characteristics coupled with microscopic observation and image analysis of the drop after heat treatment. The experiments were carried out at temperatures ranging from 20 to 80 degrees C with different thermal regimes. During the heating period, competition exists between the effect of temperature on the film fluidity and the increase in mechanical properties associated with the interfacial gelation process. During the isothermal treatment, the surface dilational modulus, E, increases, and the phase angle, delta, decreases with time to a plateau value. The frequency dependence of E and delta is characteristic of viscoelastic films with increasing delta and decreasing E at lower frequencies. The effects of heat treatment depend on the conditions at which the gelation process takes place. Microscopic observation of gelled films gives complementary information on the effect of heat treatment on WPI adsorbed films.

Gels↗
PubMed1999

Protein adsorption at the oil/water interface: characterization of adsorption kinetics by dynamic interfacial tension measurements.

The dynamics of protein adsorption at an oil/water interface are examined over time scales ranging from seconds to several hours. The pendant drop technique is used to determine the dynamic interfacial tension of several proteins at the heptane/aqueous buffer interface. The kinetics of adsorption of these proteins are interpreted from tension/log time plots, which often display three distinct regimes. (I) Diffusion and protein interfacial affinity determine the duration of an initial induction period of minimal tension reduction. A comparison of surface pressure profiles at the oil/water and air/water interface reveals the role of interfacial conformational changes in the early stages of adsorption. (II) Continued rearrangement defines the second regime, where the resulting number of interfacial contacts per protein molecule causes a steep tension decline. (III) The final regime occurs upon monolayer coverage, and is attributed to continued relaxation of the adsorbed layer and possible build-up of multilayers. Denaturation of proteins by urea in the bulk phase is shown to affect early regimes.

Adsorption↗
PubMed1999

Characterization of functional residues in the interfacial recognition domain of lecithin cholesterol acyltransferase (LCAT).

Lecithin cholesterol acyltransferase (LCAT) is an interfacial enzyme active on both high-density (HDL) and low-density lipoproteins (LDL). Threading alignments of LCAT with lipases suggest that residues 50-74 form an interfacial recognition site and this hypothesis was tested by site-directed mutagenesis. The (delta56-68) deletion mutant had no activity on any substrate. Substitution of W61 with F, Y, L or G suggested that an aromatic residue is required for full enzymatic activity. The activity of the W61F and W61Y mutants was retained on HDL but decreased on LDL, possibly owing to impaired accessibility to the LDL lipid substrate. The decreased activity of the single R52A and K53A mutants on HDL and LDL and the severer effect of the double mutation suggested that these conserved residues contribute to the folding of the LCAT lid. The membrane-destabilizing properties of the LCAT 56-68 helical segment were demonstrated using the corresponding synthetic peptide. An M65N-N66M substitution decreased both the fusogenic properties of the peptide and the activity of the mutant enzyme on all substrates. These results suggest that the putative interfacial recognition domain of LCAT plays an important role in regulating the interaction of the enzyme with its organized lipoprotein substrates.

Candida↗
PubMed1999

Contributions of residues of pancreatic phospholipase A2 to interfacial binding, catalysis, and activation.

Primary rate and equilibrium parameters for 60 site-directed mutants of bovine pancreatic phospholipase A2 (PLA2) are analyzed so incremental contributions of the substitution of specific residues can be evaluated. The magnitude of the change is evaluated so a functional role in the context of the N- and C-domains of PLA2 can be assigned, and their relationship to the catalytic residues and to the i-face that makes contact with the interface. The effect of substitutions and interfacial charge is characterized by the equilibrium dissociation constant for dissociation of the bound enzyme from the interface (Kd), the dissociation constant for dissociation of a substrate mimic from the active site of the bound enzyme (KL), and the interfacial Michaelis constants, KM and kcat. Activity is lost (>99.9%) on the substitution of H48 and D49, the catalytic residues. A more than 95% decrease in kcat is seen with the substitution of F5, I9, D99, A102, or F106, which form the substrate binding pocket. Certain residues, which are not part of the catalytic site or the substrate binding pocket, also modulate kcat. Interfacial anionic charge lowers Kd, and induces kcat activation through K56, K53, K119, or K120. Significant changes in KL are seen by the substitution of N6, I9, F22, Y52, K53, N71, Y73, A102, or A103. Changes in KM [=(k2+k-1)/k1] are attributed to kcat (=k2) and KL (=k-1/k1). Some substitutions change more than one parameter, implying an allosteric effect of the binding to the interface on KS, and the effect of the interfacial anionic charge on kcat. Interpreted in the context of the overall structure, results provide insights into the role of segments and domains in the microscopic events of catalytic turnover and processivity, and their allosteric regulation. We suggest that the interfacial recognition region (i-face) of PLA2, due to the plasticity of certain segments and domains, exercises an allosteric control on the substrate binding and chemical step.

Animals↗
PubMed1998

Characterization of permeability and network structure of interfacially photopolymerized poly(ethylene glycol) diacrylate hydrogels.

Hydrogel membranes formed by interfacially photopolymerizing poly(ethylene glycol) (PEG) diacrylate precursor solution were prepared from PEG diacrylate of molecular weights (MW) ranging from 2000 (2K) to 20000 (20K) with concentrations ranging from 10% to 30% w/w. The effects of PEG diacrylate MW and concentration in the membrane precursor solution upon the diffusivities of vitamin B12, myoglobin, ovalbumin, albumin, and IgG were determined. Regardless of the concentration of the PEG diacrylate in the precursor solution, hydrogels prepared with PEG 2K, 4K, and 8K diacrylate were impermeable to proteins with a size equal to or larger than myoglobin (22 kDa), while hydrogels prepared with PEG 20K diacrylate were impermeable to proteins with a size equal to or larger than ovalbumin (45 kDa). Similarities between hydrogels formed from PEG 2K, 4K, and 8K diacrylates were also seen in calculations of the molecular weight between crosslinks and the mesh size, with values in the range of 150-750 g/mol and 15-35 A, respectively, depending on PEG diacrylate concentration. In contrast, hydrogels formed from PEG 20K diacrylate had molecular weight between crosslinks ranging from 1150 to 2000 g/mol and mesh sizes ranging from 45-70 A, with larger values being observed in membranes polymerized from more dilute PEG diacrylate precursor.

Cross-Linking Reagents↗
PubMed2000

Characterization, at the bone crystal level, of the titanium-coating/bone interfacial zone.

Well integrated and clinically functional titanium dental implants retrieved in humans after 14 and 40 months of settlement were used for the characterization of the interfacial area between the plasma-sprayed coating and the surrounding mineralized bone. Electron microscopic studies were performed from undecalcified intact coating/bone interfaces. The concomitant presence of direct bone tissue apposition on the titanium coating, as well as the interposition of amorphous material along the same interfacial zones emphasizes the dynamic biologic aspect of the osseointegration process. A very striking finding of these ultrastructural and microanalytical investigations was the presence of tiny titanium grains ranging from 5 to 50 nm in diameter at the surface of bulky plasma-sprayed coating particles. High-resolution transmission electron microscopy revealed a continuity between the lattice planes of the coating material and those of the minute titanium grains; thus indicating a chemical binding. The thickness of the granular titanium layer interposed between coating particles and mineralized bone tissue ranged up to 600 nm. The observation of calcium-phosphate needle-like crystallites within the porous layer made of titanium grains indicates a bone ingrowth process, suggesting a bone-binding mechanism to the outer surface of the coated titanium implant.

Aged↗
PubMed1997

Disposition of amphiphilic helices in heteropolar environments.

It is known that alpha helices in globular proteins usually consist of two types of residues, hydrophobic and hydrophilic, with the number of each type being roughly equal. Except for many transmembrane helices, alpha-helices are generally amphiphilic to some degree. This is not entirely surprising because alpha-helices typically reside in heteropolar environments that arise from the polar aqueous solution that surrounds a protein and the apolar "hydrophobic core" located at its center. The packing of alpha-helices in such heteropolar environments is driven by the minimization of free energy brought about by placing hydrophobic sidechains into apolar environments and hydrophilic sidechains into polar environments. The interface between the two environments can be characterized by an interfacial plane, called the demarcation plane, that optimally separates the two classes of residues. The inclination angle omega between the axis of the helix and the demarcation plane provides a measure of the degree of amphiphilicity of an alpha-helix. For highly amphiphilic helices, omega approximately 0. The inclination angle provides a new measure of amphiphilicity that complements the hydrophobic moments of Eisenberg et al. Based on the simple physical model described above, an algorithm is developed for predicting the helix inclination angle. The calculated results show that the inclination angle for most alpha-helices extracted from globular proteins is less than 25 degrees in magnitude. This suggests that helices found in globular proteins tend to be reasonably amphiphilic with half their face dominated by hydrophobic residues and the other half by hydrophilic residues. A new two-dimensional representation that characterizes the disposition of hydrophobic and hydrophilic residues in alpha-helices, called a "wenxiang diagram," is presented. The wenxiang diagram can also be used as an important element to represent a protein molecule.

Algorithms↗
PubMed1999

Hydrolysis of monodisperse phosphatidylcholines by phospholipase A2 occurs on vessel walls and air bubbles.

Hydrolysis of monodisperse short chain phosphatidylcholines, far below their critical micelle concentration, by phospholipase A2 (PLA2) and other interfacial enzymes is characterized. Results show that virtually all the observed hydrolysis by pancreatic and human inflammatory PLA2 occurs on surfaces of the reaction vessel or air bubbles. Conditions to eliminate such extraneous contributions at low substrate concentrations are established. Premicellar aggregates are apparently formed near the critical micelle concentration. The observation window at low substrate concentrations is used to obtain an upper limit estimate of the rate of hydrolysis through the monodisperse Michaelis complex. A limit estimate of <0.1 s-1 is obtained for the hydrolysis of monodisperse substrates by pig pancreatic phospholipase A2. These results show that the observed rate of hydrolysis of dihexanoyl- and diheptanoylphosphatidylcholines with pig pancreatic phospholipase A(2) through the monomer path is insignificant compared to the rate of >1000 s-1 seen at the saturating levels of the micellar substrate. These protocols should be useful for evaluating reactions catalyzed at vessel walls. Implications of these results for assays and models of interfacial activation of pancreatic PLA2 are discussed.

Adsorption↗
PubMed2000

Unfolding pathway of the colicin E1 channel protein on a membrane surface.

The channel-forming domain of colicin E1 is composed of a soluble helical bundle which, upon membrane binding, unfolds to form an extended, two-dimensional helical net in the membrane interfacial layer. To characterize the pathway of unfolding of the protein and the structure of the surface-bound intermediate, the time-course of intra-protein distance changes and unfolding on a millisecond time-scale were determined from the kinetics of changes in the efficiency of fluorescence resonance energy transfer, and of the donor-acceptor overlap integral, between each of six individual tryptophan residues and a Cys-conjugated energy transfer acceptor (C509-AEDANS). Comparison of the rate constants revealed the following order of events associated with unfolding of the protein at the membrane surface: (A) movement of the hydrophobic core helices VIII-IX, coincident with a small change in Trp-Cys509 distances of the outer helices; (B) unfolding of surface helices in the helical bundle in the order: helix I, helices III, IV, VI, VII, and helix V; (C) a slow (time-scale, seconds) condensation of the surface-bound helices. The rate of protein unfolding events increased with increasing anionic lipid content. Unfolding did not occur below the lipid thermal phase transition, indicating that unfolding requires mobility in the interfacial layer. The structure of the two-dimensional membrane-bound intermediate in the steady-state was inferred to consist of a quasi-circular arrangement of eight helices embedded in the membrane interfacial layer and anchored by the hydrophobic helical hairpin. The pathway of unfolding of the colicin channel at the membrane surface, catalyzed by electrostatic and hydrophobic forces, is the first described for a membrane-active protein. It is proposed that the pathway and principles described for the colicin protein are relevant to membrane protein import.

Colicins↗
PubMed1976

The interaction of macromolecular solutions with macromolecular monolayers adsorbed on a hydrophobic surface.

In order to elucidate the general patterns of intermacromolecular surface interactions that may be involved in hemocompatibility phenomena, monolayers of representative macromolecules on an octadecylsilylated glass surface were exposed to solutions of other macromolecules, and the changes in interfacial composition were characterized by zeta potential-pH titration curves, as measured by alternating flow streaming current analysis and, in some cases, by radiotracer labeling. Experiments with poly(vinylpyrrolidone) (PVP), a blood-compatible linear polymer; bovine serum albumin (BSA), a representative serum protein; whole human serum (HS), a complex mixture of proteins; and erythrocyte surface glycoprotein (GP), an extended-chain macromolecular amphiphile, showed the following: 1) Penetration of the original monolayer occurred within 24 hr in 9 of the 12 possible cases; it did not occur for BSA or HS monolayers exposed to PVP, and probably not for PVP exposed to GP. 2) In all cases, penetration was accompanied by no more than partial displacement of the original monolayer, thereby generating a mixed monolayer. Each of the six possible binary mixed monolayers could be obtained by at least one of the two possible mixing sequences. 3) In the three binary systems containing BSA, the formation of the mixed monolayer could be related to increased adsorption in the two-component system. 4) The two components of the mixed monolayers were not equally distributed across their thicknesses: thus, the outer surfaces of the PVP-BSA and (at neutral pH) the PVP-HS mixed monolayers contained only PVP; that of the BSA-HS mixtures only HS. In the PVP-HS, and probably the GP-BSA and GP-HS mixed monolayers, the composition of the outer surface appeared pH-dependent. The resultant zeta potential versus pH profiles in the latter two cases resembled those of intact blood cells. The results suggest that neither the compact monolayers of globular proteins nor the diffuse monolayers of randomly coiled water-soluble polymers can, by their prior adsorption on a synthetic surface, prevent the subsequent adsorption of other globular macromolecules. It is possible that the randomly coiled polymers may impede the adhesion of platelets to the substrate since the results indicate that the adsorption of such polymers causes a displacement of the shear plane.

Adsorption↗
PubMed1986

Effect of microstructure of poly(propylene-oxide)-segmented polyamides on platelet adhesion.

The relationship between microstructure and platelet adhesivity of six types of poly(propylene oxide) (PPO)-segmented polyamides based on the polyamide segments nylon 210, 310, 410, 510, 610, and 710 were investigated. These multiblock PPO-segmented copolymers were prepared by interfacial polycondensation. Physical characterization of these copolymers was by means of thermal analysis, transmission electron microscope, wide-angle X-ray diffraction (WAXD), and small-angle X-ray scattering (SAXS). The WAXD and SAXS measurements showed that the copolymers had microstructures containing crystalline and amorphous phases and that these microstructures, represented by means of crystallite thickness and long period, varied with incorporation of PPO segments. Blood compatibility of these copolymers was evaluated by estimating the amount of adhering platelets on the copolymer surfaces. The amount of adhering platelets was minimum for the surfaces of the copolymers having a crystallite thickness of 6.0-6.5 nm and a long period of 12-13 nm. This result suggests that the particular size and distribution of the crystalline and amorphous phases in the copolymer could be determining factors for suppressing platelet adhesion on the copolymer surface, and that the control of these factors could lead to ideal antithrombogenic polymers.

Animals↗
PubMed1999

Magnetic Resonance Imaging Study of the Dissolution Kinetics of Octanol in Porous Media.

Magnetic resonance imaging (MRI) is used to visualize the dissolution of entrapped ganglia or "blobs" of octanol within the pore space of a randomly packed bed of glass ballotini, by a mobile aqueous phase. MRI provides three dimensional images, able to distinguish the solid, hydrocarbon, and aqueous phases, as well as velocity maps of the mobile aqueous phase. Dissolution of the hydrocarbon phase has been modeled using a one dimensional advection-dispersion description incorporating a mass transfer term between the hydrocarbon and aqueous phases. Essential to this mass transfer term is a description of the interfacial area between the hydrocarbon and aqueous phases which is actively involved in dissolution and which can be determined directly from the images. The experimental data are best modeled by evaluating an effective interfacial area term characterizing the hydrocarbon/water boundary which excludes the narrowest constrictions within the interparticle space. MRI visualizations of the structure of the pore space and the flow processes occurring within it, demonstrate that heterogeneities in the flow at the length-scale of individual pores within the interparticle space cause significant heterogeneity in the dissolution process which becomes significant at low hydrocarbon saturations. Copyright 1999 Academic Press.

Journal Article↗
PubMedDate not supplied

Chemical synthesis and surface activity of lung surfactant phospholipid analogs. III. Chiral N-substituted ether-amide phosphonolipids.

A homologous series of chiral (R) ether-amide phosphonolipid analogs of naturally occurring (R) glycerophospholipids were synthesized and characterized for their interfacial behaviors. The phosphonolipids possess isoteric ether, amide, and phosphonate functions at positions corresponding to the sn-1, sn-2, and sn-3 ester functions, respectively, of naturally occurring glycerophospholipids. All compounds were synthesized with disaturated C16:0 alkyl/acyl moieties to give structural analogy with dipalmitoyl phosphatidylcholine (DPPC), the major glycerophospholipid component of lung surfactant. Further substitutions at the headgroup nitrogen were also used to generate differences in headgroup size and polarity in the synthetic compounds. The surface activity of the ether-amide phospholipids was investigated in terms of adsorption to the air-water interface, together with studies of dynamic respreading after monolayer collapse and surface tension lowering in dynamically compressed spread films and dispersions. Results showed that several ether-amide phosphonolipids had more rapid adsorption and improved dynamic respreading behavior compared to DPPC, plus the ability to lower surface tension into the range of less than 1 to 4 mN/m in spread films and in dispersions under dynamic conditions. In combination with a series of diether phosphonolipids synthetized in a companion study [1], these ether-amide compounds are useful in the development of molecular structure-surface activity correlates for lung surfactant-related materials, and should assist in investigating the specificity of interactions between phospholipids and other pulmonary biological molecules.

Amides↗
PubMedDate not supplied

Pluronic F127-based ocular delivery system containing biodegradable polyisobutylcyanoacrylate nanocapsules of pilocarpine.

The objectives of our study were to prepare a biodegradable polyisobutylcyanoacrylate (PIBCA) colloidal particulate system of pilocarpine, to incorporate it into a Pluronic F127(PF127)-based gel delivery system, and to evaluate its ability to prolong the release of pilocarpine. Polyisobutylcyanoacrylate nanocapsules (PIBCA-NC) of pilocarpine were prepared by interfacial polymerization. Physicochemical characterization of the colloidal dispersion of PIBCA-NC of pilocarpine was performed by measuring drug loading, particle size analysis, and scanning electron microscopy. Results indicated that approximately 13.5% of pilocarpine was loaded onto the PIBCA-NC, the nanocapsules ranged from 370 to 460 nm, the distribution was narrow, and there was no significant effect of stirring speed on particle size. The PIBCA-NC dispersion of 1% pilocarpine alone (I) and after incorporation into the Pluronic F127 gel delivery system (II) were compared against 1% pilocarpine incorporated into a PF127 gel containing 5% methylcellulose (PF127MC) alone (III) by measuring the miotic response in the albino rabbit eye. Statistical analysis indicated a rank-order for both the duration and intensity of miosis of II > III >> I, with all differences being significant (p < 0.05). Thus, it appears that II increases the contact time of pilocarpine with the absorbing tissue in the eye, thereby improving ocular bioavailability. The PIBCA-NC of pilocarpine dispersed in the PF127MC gel delivery system has considerable potential for achieving a prolonged delivery for such drugs as pilocarpine and other more hydrophobic drugs.

Algorithms↗
PubMed1999

Biophysical characterization and modeling of lung surfactant components.

The present study characterizes the dynamic interfacial properties of calf lung surfactant (CLS) and samples reconstituted in a stepwise fashion from phospholipid (PL), hydrophobic apoprotein (HA), surfactant apoprotein A (SP-A), and neutral lipid fractions. Dipalmitoylphosphatidylcholine (DPPC), the major PL component of surfactant, was examined for comparison. Surface tension was measured over a range of oscillation frequencies (1-100 cycles/min) and bulk phase concentrations (0.01-1 mg/ml) by using a pulsating bubble surfactometer. Distinct differences in behavior were seen between samples. These differences were interpreted by using a previously validated model of surfactant adsorption kinetics that describes function in terms of 1) adsorption rate coefficient (k1), 2) desorption rate coefficient (k2), 3) minimum equilibrium surface tension (gamma*), 4) minimum surface tension at film collapse (gammamin), and 5) change in surface tension with interfacial area for gamma < gamma* (m2). Results show that DPPC and PL have k1 and k2 values several orders of magnitude lower than CLS. PL had a gammamin of 19-20 dyn/cm, significantly greater than CLS (nearly zero). Addition of the HA to PL restored dynamic interfacial behavior to nearly that of CLS. However, m2 remained at a reduced level. Addition of the SP-A to PL + HA restored m2 to a level similar to that of CLS. No further improvement in function occurred with the addition of the neutral lipid. These results support prior studies that show addition of HA to the PL markedly increases adsorption and film stability. However, SP-A is required to completely normalize dynamic behavior.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1993

Quantitative contribution of resin infiltration/hybridization to dentin bonding.

This study determined, quantitatively, the role of resin infiltration in dentin bonding. Four groups contained 10 molar teeth. Thirty were sectioned in the mid-coronal region and the dentin ground flat with 600 grit silicon carbide paper. Group 1: smear layer intact; Group 2: smear layer removed with a Prophy Jet; Group 3: conditioned with 10% H3PO4 for 20 seconds; Group 4: comprised dentin exposed by a transverse, mid-coronal fracture. Dentin surfaces were treated with All-Bond 2, its companion bonding agent, followed by P50 resin composite, polymerized in 1 mm increments. After storage in water at 37 degrees C for 24 hours, the assemblies were tested to failure in a shear mode at a crosshead speed of 5 mm/minute. Surface and interfacial morphology was characterized using SEM. Values in MPa were: Group 1: 10.24 +/- 2.98; Group 2: 20.37 +/- 4.62; Group 3: 32.68 +/- 7.12; and Group 4: 26.77 +/- 4.85. ANOVA and student t-test showed the means statistically different (P < 0.05). Since resin penetration was only found appreciably in dentin tubules in Group 4 and tubular and intertubular penetration in Group 3, it was concluded that resin infiltration can contribute approximately one third of the shear bond strength of this total etch system.

Acid Etching, Dental↗