Interviewing patients using interpreters in an oncology setting: initial evaluation of a communication skills module.

OBJECTIVES: To develop a communication skills training (CST) module for health care professionals, particularly in the area of oncology, on how to conduct interviews using interpreters and to evaluate the module in terms of participant's self-efficacy and satisfaction. METHODS: Forty-seven multi-specialty health care providers from the New York Metropolitan Area attended a communication skills module at a Comprehensive Cancer Care Center about how to conduct clinical interviews utilizing interpreters. The development of this module was on the basis of current literature and followed the Comskil model previously utilized for other doctor-patient CSTs. Participants were given pre- and post-surveys to evaluate their own confidence as well as the helpfulness of the module. RESULTS: On the basis of a retrospective pre-post measure, participants reported an increase in their confidence about interviewing patients via translators. In addition, at least 80% of participants reported their satisfaction with the various components of the module by either agreeing or strongly agreeing with the different statements. CONCLUSIONS: We have developed a module that trains clinicians in effective collaboration with professional medical interpreters and shown its ability to increase the confidence of clinician's to work with limited English proficiency patients. Our approach intends to minimize not only the language barrier but also the cultural barriers that could potentially interfere with patients' care. PRACTICE IMPLICATIONS: This work has important practice implications in the oncology setting, where cultural sensitivity is paramount and empathic exchange with the patient optimizes their sense of being well supported by their health care team. We believe that this model is generalizable to many other medical settings where use needs to be made of a professional interpreter.

Plague outbreak in the Libyan Arab Jamahiriya.

Plague is circulating regularly in localised areas worldwide, causing sporadic cases outside Africa and remains endemic or causes limited outbreaks in some African countries. Furthermore, some notable outbreaks have been reported in Asia in the last 20 years. A limited outbreak with five cases has recently been notified by the health authorities of the Libyan Arab Jamahiriya.

The 2009 pandemic H1N1 influenza and indigenous populations of the Americas and the Pacific.

There are few structured data available to assess the risks associated with pandemic influenza A(H1N1)v infection according to ethnic groups. In countries of the Americas and the Pacific where these data are available, the attack rates are higher in indigenous populations, who also appear to be at approximately three to six-fold higher risk of developing severe disease and of dying. These observations may be associated with documented risk factors for severe disease and death associated with pandemic H1N1 influenza infection (especially the generally higher prevalence of diabetes, obesity, asthma, chronic obstructive pulmonary disease and pregnancy in indigenous populations). More speculative factors include those associated with the risk of infection (e.g. family size, crowding and poverty), differences in access to health services and, perhaps, genetic factors. Whatever the causes, this increased vulnerability of indigenous populations justify specific immediate actions in the control of the current pandemic including primary prevention (intensified hygiene promotion, chemoprophylaxis and vaccination) and secondary prevention (improved access to services and early treatment following symptoms onset) of severe pandemic H1N1 influenza infection.

Characterisation and foaming properties of hydrolysates derived from rapeseed isolate.

Two hydrolysis methods used to obtain rapeseed isolate derivates were compared: chemical hydrolysis performed under alkaline conditions and pepsic proteolysis performed under acidic conditions. The mean molecular weights obtained for the hydrolysates varied from 26 to 2.5 kDa, depending on the level of hydrolysis. Further characterisation showed that, at the same level of hydrolysis, the chemical hydrolysates differed by their charges and hydrophobicity from those derived from enzymatic digestion. Analysis of the foaming properties showed, for both cases, that a limited degree of hydrolysis, around 3%, was sufficient to optimise the foaming properties of the isolate despite the different physicochemical properties of the peptides generated. The study of foaming properties at basic, neutral and acidic pHs showed that the hydrolysate solutions yielded dense foams which drained slowly and which maintained a very stable volume under the three pH conditions tested.

Conformational changes upon dissociation of a globular protein from pea: a Fourier transform infrared spectroscopy study.

Fourier transform infrared spectroscopy shows that the secondary structure of legumin, a globular protein from pea seeds, is composed of 41% beta-sheets and 16% alpha-helices and furthermore reveals the presence of beta-turns. The conformation prediction from the analysis of the amino-acid sequence of legumin using hydrophobic cluster analysis reveals that the C-terminal part of the alpha-polypeptide is devoid of defined secondary structures, whereas the beta-polypeptide is highly ordered. Comparison with analogous 11S globulins from other plant families indicates that ordered domains are highly preserved, phenomenon that may be associated with the similarity of the quaternary structure of these proteins. The results also reveal the presence of a large hypervariable region, located at the surface of the protein, that could be at the origin of the different functional properties of the 11S type globulins. The step-by-step destruction of the quaternary oligomeric structure of the native protein is accompanied by conformational changes that depend on the dissociation conditions. Whereas acylation leads to a decrease of the alpha-helix content by 10% at the expense of the beta-sheet content, addition of sodium perchlorate results in the conversion of 10% of the protein secondary structure from beta-sheet to unordered. These observations provide further evidence of the existence of different monomeric states that differ from their secondary structure and, therefore, exhibit different surface-active properties.

Structural characteristics of a globular protein investigated by X-ray photoelectron spectroscopy: comparison between a legumin film and a powdered legumin.

Films of legumin, a pea protein, were deposited onto a glass support using the Langmuir-Blodgett method, at various surface pressures. XPS study of these films show that their thickness increases with the deposition pressure. At the pressure limits of films stability, the thickness values (respectively 73 and 110 A) are close to the protein dimensions. Layered at low pressure, the oblate protein stands up when pressure increases. Furthermore, XPS study shows that the orientation of the external flexible loops depends on the obtention conditions. Thus, in the case of Langmuir-Blodgett films, hydrophobic residues are turned towards the external surface, and the hydrophilic ones towards the glass substrate. But, in the opposite, when protein is obtained by lyophilization, the hydrophilic residues are orientated outsides. It seems possible to determine by XPS the nature of the residues which give to the protein its reactivity, since they are located at its external surface.

Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds.

The trypsin/chymotrypsin inhibitors from winter pea seeds (PsTI) are members of the Bowman-Birk protease inhibitor (BBPI) family. The crystal structure of the isoform PsTI-IVb was determined by molecular replacement at 2.7 A resolution using the X-ray co-ordinates of the soybean inhibitor as a search model. The inhibitor crystallized with a nearly perfect 2-fold symmetric dimer in the asymmetric unit. Although the overall structure is very similar to that seen in other BBPIs, there are notable new structural features. Unlike the previously reported X-ray structures of BBPIs, the structure of PsTI-IVb includes the C-terminal segment of the molecule. The C-terminal tail of each subunit is partly beta-stranded and interacts with the 2-fold symmetry-related subunit, forming a beta-sheet with strands A and B of this subunit. The dimer is mainly stabilized by a large internal hydrogen-bonded network surrounded by two hydrophobic links. Fluorescence anisotropy decay measurements show that residues Tyr59 and Tyr43 are mobile in the picosecond time scale with a large amplitude. The fluorescence study and a molecular model of the simultaneous binding of PsTI-IVb to porcine trypsin and bovine chymotrypsin are compatible only with a monomeric state of the functional molecule in solution.

Large scale purification of rapeseed proteins (Brassica napus L.).

Rapeseed (Brassica napus L.) cruciferin (12S globulin), napin (2S albumin) and lipid transfer proteins (LTP) were purified at a multi-g scale. The procedure developed was simple, rather fast and resolutive; it permitted the recovery of these proteins with a good yield, such as 40% for cruciferin and 18% for napin. Nanofiltration eliminated the major phenolic compounds. The remaining protein fraction was fractionated by cation exchange chromatography (CEC) on a streamline SP-XL column in alkaline conditions. The unbound neutral cruciferin was polished by size exclusion chromatography. The alkaline napin isoforms and LTP, adsorbed on the beads, were eluted as a whole fraction and further separated by an other CEC step at acidic pH. Napins were polished by hydrophobic interaction chromatography (HIC). The fractions were characterized by reverse phase HPLC, electrophoresis, N-terminal sequencing and mass spectrometry. All the fractions contained less than 5% of impurities.

Effect of pea and bovine trypsin inhibitors on wild-type and modified trypsins.

In order to modify the catalytic properties of trypsin, lysine-188 (S1) of the substrate binding pocket was substituted by an aromatic amino acid residue (Phe, Tyr, Trp) or by a histidyl residue. Two other mutants were obtained by displacement or elimination of the negative charge of aspartic acid-189 (K188D/D189K and G187W/K188F/D189Y, respectively). The high affinity inhibitors, like PSTI II and BPTI, behaved as specific substrates of the trypsin and its mutants. Their inhibiting effect toward modified trypsins was studied. The bovine inhibitor had a higher affinity for all tested enzymes than pea inhibitor. The inhibition constants differed according to the mutations on the protease.

Betulinic acid derivatives: a new class of human immunodeficiency virus type 1 specific inhibitors with a new mode of action.

A series of omega-undecanoic amides of lup-20(29)-en-28-oic acid derivatives were synthesized and evaluated for activity in CEM 4 and MT-4 cell cultures against human immunodeficiency virus type 1 (HIV-1) strain IIIB/LAI. The potent HIV inhibitors which emerged, compounds 5a, 16a, and 17b, were all derivatives of betulinic acid (3beta-hydroxylup-20(29)-en-28-oic acid). No activity was found against HIV-2 strain ROD. Compound 5a showed no inhibition of HIV-1 reverse transcriptase activity with poly(C).oligo(dG) as template/primer, nor did it inhibit HIV-1 protease. Additional mechanistic studies revealed that this class of compounds interfere with HIV-1 entry in the cells at a postbinding step.

Wheat prolamine crosslinking through dityrosine formation catalyzed by peroxidases: improvement in the modification of a poorly accessible substrate by "indirect" catalysis

"Enzyme-assisted" oxidative polymerization of wheat gliadins was performed in an attempt to obtain new protein-based networks. Two plant peroxidases (soybean and horseradish) were used to induce the dimerization of tyrosine residues. The results show that tyrosines are poorly modified by these enzymes in an aqueous medium (dityrosine corresponded to 2% of the total amount of tyrosine). Two approaches were tested to overcome problems relating to accessibility to the target tyrosines: First, the efficiency of protein crosslinking via tyrosine-tyrosine aromatic ring condensation was enhanced in water when the proteins were oxidized by a fungus peroxidase (manganese-dependent peroxidase from Phanerochaete chrysosporium), which acts according to an indirect catalysis mechanism (up to 12% of the total amount of tyrosine is recovered under a dimeric form). Second, when the gliadins were dispersed in a water/dioxane (3/1) mixed solvent system, the tyrosines were more accessible on the protein surface, and similar yields were obtained with both types of peroxidase. The two types of catalysis (contact and indirect) are considered from the standpoint of the accessibility of the target residues. Enzymatic oxidations were also performed on synthetic peptides mimicking the repeatitive domains of gliadins. The results show that exposure of tyrosine to the solvent may not be sufficient to induce dityrosine formation. The mechanical properties of some films obtained from peroxidase-treated gliadins were investigated to correlate protein crosslinking with a potential application. One effect of the enzymatic treatment was to increase the tensile strength of the films. Copyright 1999 John Wiley & Sons, Inc.

Adaptive immune responses of legumin nanoparticles.

Legumin is one of the main storage proteins in the pea seeds (Pisum sativum L.) and the molecules of this protein have the capacity of binding together to form nanoparticles after aggregation and chemical cross-linkage with glutaraldehyde. The aim of this work was to study the adaptive immune response of legumin nanoparticles in rats. Following intradermal immunisation with the native protein legumin and legumin nanoparticles of about 250 nm, the humoral and cell-mediated immune responses were analysed in rats. The humoral responses against legumin and legumin nanoparticles were examined by western blot and ELISA analysis. Both techniques clearly showed that sera from rats immunised with legumin strongly expressed antibodies against this protein. On the contrary, serum samples from rats inoculated with legumin nanoparticles did not contain detectable amounts of antibodies. These results may be explained by a reduction on the antigenic epitopes of the protein induced by the glutaraldehyde used during the cross-linking step. Concerning the cell-mediated response, neither legumin nor legumin nanoparticles stimulated an immunogenic response. This absence of response of spleen lymphocytes for legumin and legumin nanoparticles may be explained by a cytostatic effect of legumin which was corroborated by the evaluation of the middle phase of cell apoptose. In fact, both legumin and legumin nanoparticles are potent inductors of a cytostatic phenomenon and showed a significant increase of the chromatin condensation (p < 0.05) as compared with control.

Surface functional properties of native, acid-treated, and reduced soy glycinin. 1. Foaming properties.

Foaming properties of native and chemically modified glycinin were evaluated. Effects of ionic strength and glycinin composition and concentration on foam formation and stabilization were studied. Glycinin was modified by means of combined treatments: cold or hot acidic treatments, with or without later disulfide bridges reduction. Modified proteins obtained from glycinin present different degrees of dissociation, deamidation, and as consequence, varied surface hydrophobicity and molecular size. Parameters of forming and stabilizing of foam were correlated with both deamidation and dissociation degrees of modified and native glycinin samples. A positive relationship was observed between surface behavior and foaming properties of different protein species. Results show that dissociation, deamidation, and reduction have produced structural changes on glycinin (increased surface hydrophobicity, increased net charge, decreased molecular size) which enhance the adsorption and anchorage of proteins at the air-water interface and, consequently, improve the foam forming and stabilizing capacities.

Surface functional properties of native, acid-treated, and reduced soy glycinin. 2. Emulsifying properties.

Emulsifying properties of native and chemically modified soy glycinins were studied. The influence of ionic strength, protein sample composition and concentration, and assay conditions on the flocculation-creaming process and coalescence resistance was analyzed. Differences in these emulsifying properties were exhibited by native glycinins, which have a variable content of 4S, 11S, and 15S forms. Structure and functionality of native glycinin were modified by means of combined treatments: mild acidic treatments without heating or with heating at variable time and with or without disulfide bonds reduction. Modified glycinins presented different degrees of deamidation, surface hydrophobicity, and molecular mass. A slight enhancement of emulsifying stability at moderated deamidation degrees was observed. In different protein samples, a positive relationship between the flocculation-creaming rate constant and equilibrium oil volume fraction of emulsions with surface hydrophobicity was detected. A remarkable difference was observed between reduced and nonreduced samples, mainly with respect to behavior at low or high ionic strength.

Evolution of wheat gliadins conformation during film formation: a fourier transform infrared study.

The secondary structures of wheat gliadins (a major storage protein fraction from gluten) in film-forming solutions and their evolution during film formation were investigated by Fourier transform infrared spectroscopy. In the film-forming solution, wheat gliadins presented a mixture of different secondary structures, with an important contribution of beta-turns induced by proline residues. The presence of plasticizer did not have any influence on protein secondary structure in the film-forming solution. The evolution of protein conformation was followed during drying; the major feature of this evolution was a clear growing of the infrared band at 1622 cm(-1), characteristic of intermolecular hydrogen-bonded beta-sheets. This revealed the formation of protein aggregates during film drying. The influence of the drying temperature on film properties and gliadin secondary structures was also investigated. Higher drying temperatures induced an increase of both the tensile strength of the films and the amount of beta-sheets aggregates. Although the appearance of heat-induced disulfide bridge cross-links has already been described, there is clear evidence that hydrogen-bonded beta-sheets aggregates are also induced by thermal treatment. It was not possible, however, to determine whether there is a direct relationship between the occurrence of these aggregates and the increase of the tensile strength of the films.

Properties of deamidated gluten films enzymatically cross-linked.

Films were prepared at neutral pH from deamidated gluten by casting with or without enzymatic treatment by transglutaminase in the presence of various concentrations of diamines added to the film-forming solution. Variation in the glycerol/deamidated gluten ratio from 0.2 to 0.5 had a major effect on the film mechanical properties, which is characteristic of a plasticizing effect. A ratio of 0.35, producing a tensile strength of 1.14 +/- 0.12 MPa and an elongation at break of 376 +/- 62%, was chosen for most of the enzymatic modifications. The action of transglutaminase with or without the addition of external diamines induced a simultaneous increase in tensile strength and elongation at break of the films but tended to decrease the contact angle between the film surface and a water droplet. The presence of diamines in the film solution affected the elongation at break more than the tensile strength of the films. These diamines, able to react at their two extremities, probably acted as spacers between gluten proteins. The decrease in solubility was related to the formation of high molecular weight polymers in the film. The film properties were unaffected by the type of diamine added as secondary substrate in the transglutaminase reaction.

Molecular determinants of the influence of hydrophilic plasticizers on the mechanical properties of cast wheat gluten films.

The influence of a set of hydrophilic plasticizers varying in their chain length (ethyleneglycol and longer molecules) on the tensile strength and elongation at break of cast gluten films was studied. When considered on a molar basis (moles of plasticizer per mole of amino acid), the effect of the different plasticizers depended on their respective molecular weights for plasticizer/amino acid ratios in the range from 0.10 to 0.40. However, above a ratio of 0.40-0.50 mol/mol of amino acid, these differences were abolished and both stress and strain reached a plateau value, with all plasticizers studied. In fact, when a homologous series of molecules was considered, the ability for plasticizer to decrease stress and increase strain was closely related to the number of hydrogen bonds the molecule was able to share with the protein network. Ethyleneglycol's efficiency was, however, lower than expected from its hydrogen-bonding potential; a comparison with other diols demonstrated that this was due to the small size of this molecule. The particular effect of glycerol concentration on the films' mechanical properties suggested that other molecular features of the plasticizer, such as the number and position of hydroxide groups in the molecule, were involved in the plasticization mechanism.

Preparation and characterization of films from pea protein.

The conditions for protein film preparation from an alkaline dispersion of a pea protein isolate were investigated in the presence of polyols as plasticizers. Mechanical and barrier properties of resulting films were studied as a function of protein dispersion conditions, protein and plasticizer concentrations and ratios, chain length of the plasticizer, and pH and composition of the alkaline medium. Neither the mode of protein hydration nor the pea isolate origin had a significant effect on the mechanical properties of pea protein films. However, increasing the plasticizer chain length induced slightly higher surface hydrophobicity but poor mechanical properties. Addition of monoglycerides to film-forming solution allowed a significant improvement of the films during aging. Both tensile strength and surface hydrophobicity increased when ammonium hydroxide was used as protein dispersing agent instead of sodium hydroxide.

Grafting of aliphatic and aromatic probes on rapeseed 2S and 12S proteins: influence on their structural and physicochemical properties.

Lysyl residues of rapeseed napin (2S) and cruciferin (12S) were acylated and sulfamidated by means of anhydrides and sulfonyl chlorides, respectively. The secondary and tertiary structures as well as the surface hydrophobicity of the modified proteins were studied using circular dichroism, intrinsic fluorescence, and binding of anilinonaphthalenesulfonic acid. The results showed clearly that grafting of hydrophobic chains induced different structural modifications and surface hydrophobicities on the monomeric (2S) and on the hexameric (12S) proteins. Thus, the original structure of the 2S modified protein seemed to be preserved. Therefore, the surface hydrophobicity increased proportionally with the number of groups grafted. Conversely, after modification, 12S was shown to be expanded. As a result, hydrophobic regions were exposed, leading to a much greater hydrophobization of the protein surface. Acylation and sulfamidation appeared, therefore, to be good methods to hydrophobize efficiently the surface of the two proteins and thus might probably induce new functional properties.

Biopolymeric colloidal carriers for encapsulation or controlled release applications.

Biopolymers represent an interesting alternative to synthetic polymers in order to be used as structured carriers for controlled release and encapsulation applications. In particular, the ability of these carriers to entrap both hydrophilic and hydrophobic drugs may be very promising for many applications. In addition, the absence of chemical compounds and organic solvents used to produce biopolymeric matrices could be very interesting for some industrial applications. Simple or complex coacervation methods involving proteins or protein and polysaccharide mixtures were used to create new matrices dedicated to controlled release applications. Controlled release experiments with model compounds were conducted in order to evaluate the performance of such matrices. An alternative and promising research field deals with particles obtained from hydrogel systems. Totally transparent solid matrices resulting from the dehydration of new protein gels were formed and swelling capacities of these matrices were studied.