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Hydrophobic Interactions (hydrophobic + interaction)
Terms modified by Hydrophobic Interactions Selected AbstractsSynthetic Hydrophilic Materials with Tunable Strength and a Range of Hydrophobic Interactions,ADVANCED FUNCTIONAL MATERIALS, Issue 14 2010Olha Hoy Abstract The ability to vary, adjust, and control hydrophobic interactions is crucial in manipulating interactions between biological objects and the surface of synthetic materials in aqueous environment. To this end a grafted polymer layer (multi-component mixed polymer brush) is synthesized that is capable of reversibly exposing nanometer-sized hydrophobic fragments at its hydrophilic surface and of tuning, turning on, and turning off the hydrophobic interactions. The reversible switching occurs in response to changes in the environment and alters the strength and range of attractive interactions between the layer and hydrophobic or amphiphilic probes in water. The grafted layer retains its overall hydrophilicity, while local hydrophobic forces enable the grafted layer to sense and attract the hydrophobic domains of protein molecules dissolved in the aqueous environment. The hydrophobic interactions between the material and a hydrophobic probe are investigated using atomic force microscopy measurements and a long-range attractive and contact-adhesive interaction between the material and the probe is observed, which is controlled by environmental conditions. Switching of the layer exterior is also confirmed via protein adsorption measurements. [source] Capillary electrochromatography with zwitterionic stationary phase on the lysine-bonded poly(glycidyl methacrylate- co -ethylene dimethacrylate) monolithic capillary columnELECTROPHORESIS, Issue 12 2006Xiaoli Dong Abstract A polymer-based neutral monolithic capillary column was prepared by radical polymerization of glycidyl methacrylate and ethylene dimethacrylate in a 100,,m id fused-silica capillary, and the prepared monolithic column was subsequently modified based on a ring opening reaction of epoxide groups with 1,M,lysine in solution (pH,8.0) at 75°C for 10,h to produce a lysine chemically bonded stationary phases in capillary column. The ring opening reaction conditions were optimized so that the column could generate substantial EOF. Due to the zwitterionic functional groups of the lysine covalently bonded on the polymer monolithic rod, the prepared column can generate cathodic and anodic EOF by varying the pH values of running buffer during CEC separation. EOF reached the maximum of ,2.0×10,8,m2v,1s,1 and 2.6×10,8,m2v,1s,1 with pH of the running buffer of 2.25 and 10, respectively. As a consequence, neutral compounds, ionic solutes such as phenols, aromatic acids, anilines, and basic pharmaceuticals were all successfully separated on the column by CEC. Hydrophobic interaction is responsible for separation of neutral analytes. In addition, the electrostatic and hydrophobic interaction and the electrophoretic migration play a significant role in separation of the ionic or ionizable analytes. [source] DNA Hybrid Nanomachines: Fullerene Attachment Enhances Performance of a DNA Nanomachine (Adv. Mater.ADVANCED MATERIALS, Issue 19 200919/2009) The image shows the developing biocompatible molecules with controllable, accurate, and reproducible molecular motor functions for mobile nanodevices. Seon Jeong Kim and co-workers show on page 1907 that the attachment of fullerene moieties to a single-strand DNA significantly improves the molecular switching and stability of this pH driven enthalpic molecular machine. Hydrophobic interactions between the terminal fullerenes in the folded i-motif conformation increased the machines power stroke and force generated. [source] Effect of Ultra-high-pressure Homogenization on Structure and on Rheological Properties of Soy Protein-stabilized EmulsionsJOURNAL OF FOOD SCIENCE, Issue 9 2002J. Floury ABSTRACT: An ultra high-pressure homogenizer (20 to 350 MPa) was used to realize fine food emulsions stabilized by soy proteins. The first aim of the work was to understand how dynamic high-pressure processing affects soybean globulin conformation. Then, the effect of homogenizing pressure on the emulsions structure and rheology was investigated. High-pressure homogenization caused denaturation of proteins due to strong mechanical forces and high temperatures encountered in the valve. Droplet sizes of emulsions were greatly reduced with high-pressure homogenization and Newtonian liquid emulsions were converted into shear-thinning emulsion gels by homogenization at pressures above 250 MPa. Hydrophobic interactions between proteins were supposed to cause the gel-like network structure of emulsions. [source] Structure of murine angiogenin: features of the substrate- and cell-binding regions and prospects for inhibitor-binding studiesACTA CRYSTALLOGRAPHICA SECTION D, Issue 12 2005Daniel E. Holloway Angiogenin is an unusual member of the pancreatic ribonuclease superfamily that induces blood-vessel formation and is a promising anticancer target. The three-dimensional structure of murine angiogenin (mAng) has been determined by X-ray crystallography. Two structures are presented: one is a complex with sulfate ions (1.5,Å resolution) and the other a complex with phosphate ions (1.6,Å resolution). Residues forming the putative B1, P1 and B2 subsites occupy positions similar to their hAng counterparts and are likely to play similar roles. The anions occupy the P1 subsite, sulfate binding conventionally and phosphate adopting two orientations, one of which is novel. The B1 subsite is obstructed by Glu116 and Phe119, with the latter assuming a less invasive position than its hAng counterpart. Hydrophobic interactions between the C-terminal segment and the main body of the protein are more extensive than in hAng and may underly the lower enzymatic activity of the murine protein. Elsewhere, the structure of the H3,B2 loop supports the view that hAng Asn61 interacts directly with cell-surface molecules and does not merely stabilize adjacent regions of the hAng structure. mAng crystals appear to offer small-molecule inhibitors a clear route to the active site and may even withstand a reorientation of the C-terminal segment that provides access to the cryptic B1 subsite. These features represent considerable advantages over crystalline hAng and bAng. [source] Two alternative modes for optimizing nylon-6 byproduct hydrolytic activity from a carboxylesterase with a ,-lactamase fold: X-ray crystallographic analysis of directly evolved 6-aminohexanoate-dimer hydrolasePROTEIN SCIENCE, Issue 8 2009Taku Ohki Abstract Promiscuous 6-aminohexanoate-linear dimer (Ald)-hydrolytic activity originally obtained in a carboxylesterase with a ,-lactamase fold was enhanced about 80-fold by directed evolution using error-prone PCR and DNA shuffling. Kinetic studies of the mutant enzyme (Hyb-S4M94) demonstrated that the enzyme had acquired an increased affinity (Km = 15 mM) and turnover (kcat = 3.1 s,1) for Ald, and that a catalytic center suitable for nylon-6 byproduct hydrolysis had been generated. Construction of various mutant enzymes revealed that the enhanced activity in the newly evolved enzyme is due to the substitutions R187S/F264C/D370Y. Crystal structures of Hyb-S4M94 with bound substrate suggested that catalytic function for Ald was improved by hydrogen-bonding/hydrophobic interactions between the AldCOOH and Tyr370, a hydrogen-bonding network from Ser187 to AldNH, and interaction between AldNH and Gln27-O, derived from another subunit in the homo-dimeric structure. In wild-type Ald-hydrolase (NylB), Ald-hydrolytic activity is thought to be optimized by the substitutions G181D/H266N, which improve an electrostatic interaction with AldNH (Kawashima et al., FEBS J 2009; 276:2547,2556). We propose here that there exist at least two alternative modes for optimizing the Ald-hydrolytic activity of a carboxylesterase with a ,-lactamase fold. [source] Macrocyclic polyamine-modified poly(glycidyl methacrylate- co -ethylene dimethacrylate) monolith for capillary electrochromatographyELECTROPHORESIS, Issue 11 2008Yun Tian Abstract 1,4,10,13,16-Pentaazatricycloheneicosane-9,17-dione (macrocyclic polyamine)-modified polymer-based monolithic column for CEC was prepared by ring opening reaction of epoxide groups from poly(glycidyl methacrylate- co -ethylene dimethacrylate) (GMA- co -EDMA) monolith with macrocyclic polyamine. Conditions such as reaction time and concentration of macrocyclic polyamine for the modification reaction were optimized to generate substantial EOF and enough chromatographic interactions. Anodic EOF was observed in the pH range of 2.0,8.0 studied due to the protonation of macrcyclic polyamine at the surface of the monolith. Morphology of the monolithic column was examined by SEM and the incorporation of macrocyclic polyamine to the poly(GMA- co -EDMA) monolith was characterized by infrared (IR) spectra. Successful separation of inorganic anions, isomeric benzenediols, and benzoic acid derivatives on the monolithic column was achieved for CEC. In addition to hydrophobic interaction, hydrogen bonding and electrostatic interaction played a significant role in the separation process. [source] Capillary electrochromatography with zwitterionic stationary phase on the lysine-bonded poly(glycidyl methacrylate- co -ethylene dimethacrylate) monolithic capillary columnELECTROPHORESIS, Issue 12 2006Xiaoli Dong Abstract A polymer-based neutral monolithic capillary column was prepared by radical polymerization of glycidyl methacrylate and ethylene dimethacrylate in a 100,,m id fused-silica capillary, and the prepared monolithic column was subsequently modified based on a ring opening reaction of epoxide groups with 1,M,lysine in solution (pH,8.0) at 75°C for 10,h to produce a lysine chemically bonded stationary phases in capillary column. The ring opening reaction conditions were optimized so that the column could generate substantial EOF. Due to the zwitterionic functional groups of the lysine covalently bonded on the polymer monolithic rod, the prepared column can generate cathodic and anodic EOF by varying the pH values of running buffer during CEC separation. EOF reached the maximum of ,2.0×10,8,m2v,1s,1 and 2.6×10,8,m2v,1s,1 with pH of the running buffer of 2.25 and 10, respectively. As a consequence, neutral compounds, ionic solutes such as phenols, aromatic acids, anilines, and basic pharmaceuticals were all successfully separated on the column by CEC. Hydrophobic interaction is responsible for separation of neutral analytes. In addition, the electrostatic and hydrophobic interaction and the electrophoretic migration play a significant role in separation of the ionic or ionizable analytes. [source] Thermodynamics of the folding of D-glyceraldehyde-3-phosphate dehydrogenase assisted by protein disulfide isomerase studied by microcalorimetryFEBS JOURNAL, Issue 15 2001Yi Liang Thermodynamics of the refolding of denatured d -glyceraldehyde 3-phosphate dehydrogenase (GAPDH) assisted by protein disulfide isomerase (PDI), a molecular chaperone, has been studied by isothermal microcalorimetry at different molar ratios of PDI/GAPDH and temperatures using two thermodynamic models proposed for chaperone,substrate binding and chaperone-assisted substrate folding, respectively. The binding of GAPDH folding intermediates to PDI is driven by a large favorable enthalpy decrease with a large unfavorable entropy reduction, and shows strong enthalpy,entropy compensation and weak temperature dependence of Gibbs free energy change. A large negative heat-capacity change of the binding, ,156 kJ·mol,1·K,1, at all temperatures examined indicates that hydrophobic interaction is a major force for the binding. The binding stoichiometry shows one dimeric GAPDH intermediate per PDI monomer. The refolding of GAPDH assisted by PDI is a largely exothermic reaction at 15.0,25.0 °C. With increasing temperature from 15.0 to 37.0 °C, the PDI-assisted reactivation yield of denatured GAPDH upon dilution decreases. At 37.0 °C, the spontaneous reactivation, PDI-assisted reactivation and intrinsic molar enthalpy change during the PDI-assisted refolding of GAPDH are not detected. [source] Hydrophobic Functional Group Initiated Helical Mesostructured Silica for Controlled Drug Release,ADVANCED FUNCTIONAL MATERIALS, Issue 23 2008Lei Zhang Abstract In this paper a novel one-step synthetic pathway that controls both functionality and morphology of functionalized periodic helical mesostructured silicas by the co-condensation of tetraethoxysilane and hydrophobic organoalkoxysilane using achiral surfactants as templates is reported. In contrast to previous methods, the hydrophobic interaction between hydrophobic functional groups and the surfactant as well as the intercalation of hydrophobic groups into the micelles are proposed to lead to the formation of helical mesostructures. This study demonstrates that hydrophobic interaction and intercalation can promote the production of long cylindrical micelles, and that the formation of helical rod-like morphology is attributed to the spiral transformation from bundles of hexagonally-arrayed and straight rod-like composite micelles due to the reduction in surface free energy. It is also revealed that small amounts of mercaptopropyltrimethoxysilane, vinyltrimethoxysilane, and phenyltrimethoxysilane can cause the formation of helical mesostructures. Furthermore, the helical mesostructured silicas are employed as drug carriers for the release study of the model drug aspirin, and the results show that the drug release rate can be controlled by the morphology and helicity of the materials. [source] Use of associating polymers as multifunctional thickeners: studies of Their structure in aqueous solutions via nmr, qels, fluorescence, And rheology measurementsINTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Issue 5 2007Katsunori Yoshida The solution properties of an associating polymer were studied by NMR, quasi-elastic light scattering (QELS), fluorescence, and rheology measurements. An associative thickening (AT) polymer was designed having a nonionic poly(ethylene oxide) backbone with long alkyl chains at both ends to achieve high viscosity even at relatively high salt concentrations and over a wide pH range. This study focuses on the associative state of the polymer in aqueous solutions at various polymer concentrations. In a fluorescence probe study using pyrene a spectral change in the I3/I1 ratio was observed for pyrene at a polymer concentration (Cp) of 3 x 10 -4%, indicating an apparent critical concentration (cmc) of the amphiphilic polymer. The viscosity, self-diffusion coefficient (Dsel), and hydrodynamic size (Rh) distribution measurements at various Cp all suggest that there is a second transition at Cp, 0.4%. Although we observed the discontinuity in viscosity, Dsel, and Rh at Cp, 0.4%, no changes in the relaxation times (T1 and T2) were recognized for either the alkyl chain or the ethylene oxide moiety of the polymer at C p= 0.1,1%. These data suggest that there are no structural changes or phase transitions at Cp, 0.4%, but that intermicellar networks are presumably formed by bridging of the end alkyl groups of the polymer, which is driven by hydrophobic forces. Because the polymer forms networks by hydrophobic interaction and the polymer itself is nonionic, the viscosity of the polymer solution was influenced very little by either the addition of salt or a pH change, as would be expected. The dynamic viscoelastic study revealed that the polymer solution exhibits a single mode Maxwell type relaxation behavior with a terminal relaxation time of about 0.61 s, which imparts a unique flow appearance to the polymer solutions. The time course measurements of the dynamic elastic modulus of the stratum corneum revealed that the polymer has excellent potential for skin softening. It was concluded that the associative thickening polymer not only is a useful thickener with a salt and pH tolerance but also has beneficial skincare effects. [source] The Planck,Benzinger thermal work function in the condensation of water vaporINTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY, Issue 15 2006Paul W. Chun Abstract Based on the Planck,Benzinger thermal work function using Chun's method, the innate temperature-invariant enthalpy at 0 K, ,H0(T0), for the condensation of water vapor as well as the dimer, trimer, tetramer, and pentamer form in the vapor phase, was determined to be 0.447 kcal mol,1 for vapor, 1.127 for the dimer, 0.555 for the trimer, 0.236 for the tetramer, and 0.079 kcal mol,1 for the pentamer using ,G(T) data reported by Kell et al. in 1968 and Kell and McLaurin in 1969. These results suggest that the predominant dimeric form is the most stable of these n -mers. Using Nemethy and Scheraga's 1962 data for the Helmholtz free energy of liquid water, the value of ,H0(T0) was determined to be 1.21 kcal mol,1. This is very close to the value for the energy of the hydrogen bond EH of 1.32 kcal mol,1 reported by Nemethy and Scheraga, using statistical thermodynamics. It seems clear that very little energy is required for interconversion between the hypothetical supercooled water vapor and glassy water at 0 K. A hypothetical supercooled water vapor at 0 K is apparently almost as highly associated as glassy water at that temperature, suggesting a dynamic equilibrium between vapor and liquid. This water vapor condensation is highly similar in its thermodynamic behavior to that of sequence-specific pairwise (dipeptide) hydrophobic interaction, except that the negative Gibbs free energy change minimum at ,Ts,, the thermal setpoint for vapor condensation, where T,S = 0, occurs at a considerably lower temperature, 270 K (below 0°C) compared with ,350 K. The temperature of condensation ,Tcond, at which ,G(T) = 0, where water vapor begins to condense, was found to be 383 K. In the case of a sequence-specific pairwise hydrophobic interaction, the melting temperature, ,Tm,, where ,G(Tm) = 0 was found to be 460 K. Only between two temperature limits, ,Th, = 99 K and ,Tcond, = 383 K, where ,G(Tcond) = 0, is the net chemical driving force favorable for polymorphism of glassy water and hypothetical supercooled water vapor. Analysis of the water vapor condensation process based on the Planck,Benzinger thermal work function confirms that a thermodynamic molecular switch occurs at 10 K, wherein a change of sign in [,Cp(T)]cond leads to a true negative minimum in the Gibbs free energy of vapor condensation, and hence a maximum in the related equilibrium constant, Kcond. © 2006 Wiley Periodicals, Inc. Int J Quantum Chem, 2006 [source] In vitro degradability and stability of hydrophobically modified pH-sensitive micelles using MPEG-grafted poly(,-amino ester) for efficient encapsulation of paclitaxelJOURNAL OF APPLIED POLYMER SCIENCE, Issue 6 2010Min Sang Kim Abstract Methoxypoly(ethylene glycol)-grafted poly(,-amino ester) was synthesized for the fabrication of pH-sensitive micelles, and these micelles were modified with deoxycholic acid to facilitate the hydrophobic interaction between the micellar core and paclitaxel. The micelle properties were studied by dynamic light scattering and fluorescence spectrometry. An in vitro degradation study showed that the synthesized polymers degraded hydrolytically within 24 h under physiological conditions. The stability of paclitaxel-loaded pH-sensitive micelles was evaluated in vitro. The introduced deoxycholic acid more stabilized the micelles at pH 7.4 compared to the micelles without modification. But the pH-sensitive region of the micelles was lowered from pH 6.8 to pH 5.8. These results indicate that pH-sensitive micelles with improved stability have great potential as hydrophobic drug carriers for tumor targeting. © 2010 Wiley Periodicals, Inc. J Appl Polym Sci, 2010 [source] Release behavior of freeze-dried alginate beads containing poly(N -isopropylacrylamide) copolymersJOURNAL OF APPLIED POLYMER SCIENCE, Issue 1 2008Jae-Hyung Choi Abstract Beads composed of alginate, poly(N -isopropylacrylamide) (PNIPAM), the copolymers of N -isopropylacrylamide and methacrylic acid (P(NIPAM- co -MAA)), and the copolymers of N -isopropylacrylamide, methacrylic acid, and octadecyl acrylate (P(NIPAM- co -MAA- co -ODA)), were prepared by dropping the polymer solutions into CaCl2 solution. The beads were freeze-dried and the release of blue dextran entrapped in the beads was observed in distilled water with time and pH. The degree of release was in the order of alginate bead < alginate/PNIPAM bead , alginate/P(NIPAM- co -MAA) bead < alginate/P(NIPAM- co -MAA- co -ODA) bead. On the other hand, swelling ratios reached steady state within 20 min, and the values were 200,800 depending on the bead composition. The degree of swelling showed the same order as that of release. Among the beads, only alginate/P(NIPAM- co -MAA- co -ODA) bead exhibited pH-dependent release. At acidic condition, inter- and intraelectrostatic repulsion is weak and P(NIPAM- co -MAA- co -ODA) could readily be assembled into an aggregate due to the prevailing hydrophobic interaction of ODA. Thus, it could block the pore of bead matrix, leading to a suppressed release. © 2008 Wiley Periodicals, Inc. J Appl Polym Sci, 2008 [source] Recovery of lipase by adsorption at the n -hexadecane,water interfaceJOURNAL OF CHEMICAL TECHNOLOGY & BIOTECHNOLOGY, Issue 11 2003Hui-Min Wang Abstract A novel separation process based on the hydrophobic adsorption at the n -hexadecane,water interface was developed for the recovery of Acinetobacter radioresistens lipase from a pre-treated fermentation broth. In a mixture containing water, lipase and n -hexadecane, a water-in-oil emulsion was formed when the n -hexadecane-to-water ratio (o/w ratio) was larger than 3, and a large amount of lipase was found to be adsorbed at the interface. Compared with the oil-in-water emulsion (occurring when o/w ratio < 3), the water-in-oil emulsion generated smaller droplets and larger interfacial area, and was more stable. The harvested emulsion phase could be centrifuged to give an aqueous, concentrated lipase solution. Adsorption of lipase at the interface could be described by the Langmuir isotherm. For lipase concentrations ranging from 8.4 to 87.2 U cm,3, a single-stage adsorption resulted in a six- to four-fold concentration and 16,45% activity recovery, where lipase concentration was the dominant factor. A method using data from a single-stage adsorption to predict multiple-stage operation was described, and the agreement between the experimental and the predicted results was good. To improve the enzyme recovery, a multiple-run adsorption process was proposed. The use of salts enhanced the hydrophobic interaction between lipase and n -hexadecane. Advantages of the proposed process include simple operation, low operational cost, environmentally friendly, no requirement for pre-concentration of the enzyme solution, and negligible enzyme denaturation. Copyright © 2003 Society of Chemical Industry [source] CHARACTERISTICS OF MUSCLE FROM TWO SPECIES OF BIGEYE SNAPPER, PRIACANTHUS TAYENUS AND PRIACANTHUS MACRACANTHUSJOURNAL OF FOOD BIOCHEMISTRY, Issue 4 2002SOOTTWAT BENJAKUL ABSTRACT Composition and some properties of muscle from two species of bigeye snapper, P. tayenus and P. macracanthus, were investigated. Both species had a similar composition with the same myofibrillar protein content. However, muscle proteins from P. tayenus had higher thermal stability than those from P. macracanthus, as indicated by the higher enthalpy for transitions as well as the lower inactivation rate constant (KD). Upon 15 days of iced storage, natural actomyosin Ca2* -ATP ase and Mg2+ -Ca2+ -ATPase activities decreased, whereas Mg2+ -EGTA-ATPase activity increased, suggesting the denaturation of myosin, actomyosin and troponin/tropomyosin complexes, respectively. Increased surface hydrophobicity and decreased sulfhydryl groups indicated the denaturation possibly occurred via hydrophobic interaction and disulfide formation. Heading and eviscerating offish retarded the denaturation and physicochemical changes of proteins during iced storage. The results indicated that a rapid and proper post harvest handling was of importance to maintain the muscle quality of bigeye snapper. [source] Architecture and performance of mesoporous silica-lipase hybrids via non-covalent interfacial adsorptionAICHE JOURNAL, Issue 2 2010Shan Lu Abstract To investigate the effects of surface property of mesoporous supports on the lipase immobilization and the performance of immobilized lipase, the mesoporous molecular sieve SBA-15 is functionalized with three organic moieties, dimethyl (DM), diisopropyl (DIP), and diisobutyl (DIB), respectively, by post-synthesis grafting and one-pot synthesis methods. Porcine pancreas lipase (PPL) is immobilized on SBA-15 supports through hydrogen bonding and hydrophobic interaction. The hydrophobic adsorption involves no active sites of PPL, and neither hyper-activation nor total inactivation occurs. The study on the intrinsic stability of PPL, including thermal stability, pH stability, and storage stability, indicates that the entrapment in mesoporous supports, and especially in organic-functionalized supports, makes PPL more resistant to temperature increment but more sensitive to pH change. The reusability investigation shows that the organic modification of mesoporous surface inhibits the enzyme leaching to some extent, resulting in a better operational stability. © 2009 American Institute of Chemical Engineers AIChE J, 2010 [source] Orexin-A is composed of a highly conserved C -terminal and a specific, hydrophilic N -terminal region, revealing the structural basis of specific recognition by the orexin-1 receptorJOURNAL OF PEPTIDE SCIENCE, Issue 7 2006Tomoyo Takai Abstract Orexins-A and B, also called hypocretins-1 and 2, respectively, are neuropeptides that regulate feeding and sleep-wakefulness by binding to two orphan G protein-coupled receptors named orexin-1 (OX1R) and orexin-2 (OX2R). The sequences and functions of orexins-A and B are similar to each other, but the high sequence homology (68%) is limited in their C -terminal half regions (residues 15,33). The sequence of the N -terminal half region of orexin-A (residues 1,14), containing two disulfide bonds, is very different from that of orexin-B. The structure of orexin-A was determined using two-dimensional homonuclear and 15N and 13C natural abundance heteronuclear NMR experiments. Orexin-A had a compact conformation in the N -terminal half region, which contained a short helix (III:Cys6-Gln9) and was fixed by the two disulfide bonds, and a helix-turn-helix conformation (I:Leu16-Ala23 and II:Asn25-Thr32) in the remaining C -terminal half region. The C -terminal half region had both hydrophobic and hydrophilic residues, which existed on separate surfaces to provide an amphipathic character in helices I and II. The nine residues on the hydrophobic surface are also well conserved in orexin-B, and it was reported that the substitution of each of them with alanine resulted in a significant drop in the functional potency at the receptors. Therefore, we suggest that they form the surface responsible for the main hydrophobic interaction with the receptors. On the other hand, the residues on the hydrophilic surface, together with the hydrophilic residues in the N -terminal half region that form a cluster, are known to make only small contributions to the binding to the receptors through similar alanine-scan experiments. However, since our structure of orexin-A showed that large conformational and electrostatical differences between orexins-A and B were rather concentrated in the N -terminal half regions, we suggest that the region of orexin-A is important for the preference for orexin-A of OX1R. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd. [source] Micelle-to-vesicle transition induced by oligonucleotide in SDS/DEAB mixed system with a net negative chargeJOURNAL OF POLYMER SCIENCE (IN TWO SECTIONS), Issue 22 2008Xia Guo Abstract Sodium dodecyl sulfate (SDS)/dodecyl triethyl ammonium bromide (DEAB) mixed micelles (with SDS in excess) can transform to vesicles only when the temperature is higher than a critical value. In this study, we report for the first time that oligonucleotide can decrease the critical temperature to a much lower value and, hence, induce micelle-to-vesicle transition. The facilitation efficiency of oligonucleotide on vesicle formation is closely dependent on its size and base composition. Moreover, the SDS/DEAB/oligonucleotide vesicles are negatively charged and the hydrophobic interaction between oligonucleotide and SDS/DEAB mixed micelles is the driving force. As, so far, the report about the facilitation effect of oligonucleotide and DNA on vesicle formation is very limited, this study may provide some helpful information for the application of DNA/amphiphile system. © 2008 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem 46: 7491,7504, 2008 [source] Synthesis and supramolecular self-assembly of thermosensitive amphiphilic star copolymers based on a hyperbranched polyether coreJOURNAL OF POLYMER SCIENCE (IN TWO SECTIONS), Issue 2 2008Haiyan Hong Abstract A novel amphiphilic thermosensitive star copolymer with a hydrophobic hyperbranched poly (3-ethyl-3-(hydroxymethyl)oxetane) (HBPO) core and many hydrophilic poly(2-(dimethylamino) ethyl methacrylate) (PDMAEMA) arms was synthesized and used as the precursor for the aqueous solution self-assembly. All the copolymers directly aggregated into core,shell unimolecular micelles (around 10 nm) and size-controllable large multimolecular micelles (around 100 nm) in water at room temperature, according to pyrene probe fluorescence spectrometry and 1H NMR, TEM, and DLS measurements. The star copolymers also underwent sharp, thermosensitive phase transitions at a lower critical solution temperature (LCST), which were proved to be originated from the secondary aggregation of the large micelles driven by increasing hydrophobic interaction due to the dehydration of PDMAEMA shells on heating. A quantitative variable temperature NMR analysis method was designed by using potassium hydrogen phthalate as an external standard and displayed great potential to evaluate the LCST transition at the molecular level. The drug loading and temperature-dependent release properties of HBPO- star -PDMAEMA micelles were also investigated by using indomethacin as a model drug. The indomethacin-loaded micelles displayed a rapid drug release at a temperature around LCST. © 2007 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem 46: 668,681, 2008 [source] Indole ring orientations of Trp189 in the ground and M intermediate states of bacteriorhodopsin as studied by polarized UV resonance Raman spectroscopy,JOURNAL OF RAMAN SPECTROSCOPY, Issue 1-3 2006Kazuhiro Asakawa Abstract Polarized resonance Raman spectroscopy provides a means for orientation analysis of proteins in aligned samples. Previously, we developed a Raman linear intensity difference (RLID) method to determine the orientations of aromatic amino acid side chains in flow-oriented or membrane-bound proteins. In this study, we have applied the RLID method to Trp189 in bacteriorhodopsin (BR), a transmembrane protein that acts as a light-driven proton pump. Among the eight Trp residues in BR, the Raman spectrum of Trp189 has been extracted by subtracting the spectrum of the Trp189 , Phe mutant from that of wild-type BR. By examining the 251.3-nm-exited polarized resonance Raman intensities of two indole ring vibrations of Trp189, the directions of the La and Bb transition moments have been determined with respect the membrane normal in the light-adapted ground state (BR568) and a photo-excited intermediate (M). Comparison of the orientations of the Trp189 indole ring derived from the La and Bb inclination angles has shown that the indole ring slightly but significantly reorients toward the ionone ring of the retinal chromophore in the M intermediate. The reorientation of Trp189 is consistent with the previous observation that helix F, on which Trp189 is located, undergoes an outward tilt and the hydrophobic interaction of Trp189 increases in the M intermediate. The RLID method combined with 251.3 nm excitation and point mutation is useful for detecting even a small reorientation of a targeted Trp residue. Copyright © 2006 John Wiley & Sons, Ltd. [source] QSAR for Inhibition of Pseudomonas Species Lipase by 1-Acyloxy-3- N-n -octylcarbamyl-benzenesMOLECULAR INFORMATICS, Issue 3 2009Shyh-Ying Chiou Abstract 1-Acyloxy-3- N-n -octylcarbamyl-benzenes (1,9) are synthesized to characterize the Quantitative Structure,Activity Relationship (QSAR) for the Third Acyl Group Binding Site (TACS) of Pseudomonas species lipase. Inhibitors 1,9 are characterized as pseudo or alternate substrate inhibitors of the enzyme. The inhibition constant (Ki) and carbamylation constant (k2) for the enzyme inhibitions by inhibitors 1,9 are determined. The carbamate carbons of the n -octylcarbamyl moieties of inhibitors 1,9 are nucleophilically attacked by the active site serine of the enzyme and the n -octylcarbamyl groups of inhibitors 1,9 are bound to the Acyl Group Binding Site (ACS) of the enzyme. Both pKi and log,k2 values are linearly corrected with the Hansch hydrophobicity , values of the substituents of the acyl moieties of inhibitors 1,7. The slopes for these corrections are 0.13 and 0.02, respectively. This result suggests that the enzyme inhibitions by inhibitors 1,7 have a common mechanism. Thus, all acyl moieties of inhibitors 1,7 should bind to the TACS of the enzyme since the acyl and carbamyl moieties of inhibitors 1,7 are meta to each other. This result also indicates that the major interaction between the acyl moiety of inhibitors 1,7 and the TACS of the enzyme is primarily the hydrophobic interaction. The more hydrophobic characters of inhibitors 1,7 are, the more tightly these inhibitors bind to the enzyme. In contrast, 1-triphenylacetoxy-3- N-n -octylcarbamyl-benzene (8) and 1-trimethylacetoxy-3- N-n -octylcarbamyl-benzene (9) do not bind to the TACS of the enzyme due to the fact that the inhibitions by both inhibitors are not linearly correlated with ,. It is possible that these two inhibitors are too bulky to fit into the TACS of the enzyme. [source] Interaction Between N-terminal Loop and , -Scaffold of Photoactive Yellow Protein,PHOTOCHEMISTRY & PHOTOBIOLOGY, Issue 4 2008Miki Harigai During the photoreaction cycle of photoactive yellow protein (PYP), a physiologically active intermediate (PYPM) is formed as a consequence of global protein conformational change. Previous studies have demonstrated that the photocycle of PYP is regulated by the N-terminal loop region, which is located across the central , -sheet from the p -coumaric acid chromophore. In this paper, the hydrophobic interaction between N-terminal loop and , -sheet was studied by characterizing PYP mutants of the hydrophobic residues. The rate constants and structural changes of the photocycle of L15A and L23A possibly participating in such an interaction were more similar to wild-type than F6A, showing that the CH/, interaction between Phe6 and Lys123 is the most essential as reported previously. To better understand the interactions between N-terminal tail and , -sheet of PYP, Phe6 and Phe121 were replaced by Cys and linked by a disulfide bond. Since the photocycle kinetics, structural change and thermal stability of F6C/F121C were similar to F6A, the CH/, interaction between Phe6 and Lys123 is not substitutable. It is likely that the detachment of position 6 from position 123 substantially alters the nature of PYP. [source] Hydrogen-bonding interaction of an alternating maleic acid,vinyl acetate copolymer with poly(ethylene glycol), polyacrylamide and poly(N -isopropylacrylamide): a comparative studyPOLYMER INTERNATIONAL, Issue 12 2003C Vasile Abstract The hydrogen-bonding interaction and interpolymer complex formation between an alternating maleic acid,vinyl acetate copolymer, (MAc- alt -VA) and poly(ethylene glycol) (PEG), polyacrylamide (PAM) or poly(N -isopropylacrylamide) (PNIPAM) in aqueous solution was potentiometrically and viscometrically investigated. MAc- alt -VA formed with PEG a strong hydrogen-bonding interpolymer complex with a compact structure, and while its interaction with PAM seems to be very weak, if any, the complex formed with PNIPAM is even stronger than that with PEG. This indicates a very important contribution of hydrophobic interaction to the formation of such hydrogen-bonding interpolymer complexes. Copyright © 2003 Society of Chemical Industry [source] Synthesis of poly(cystine bisamide)-PEG block copolymers grafted with 1-(3-aminopropyl)imidazole and their phase transition behaviorsPOLYMERS FOR ADVANCED TECHNOLOGIES, Issue 11 2008Byung Suk Jin Abstract New biodegradable and pH-sensitive block copolymers were prepared by grafting 1-(3-aminopropyl) imidazole onto a backbone polymer formed via condensation polymerization between l -cystine and EDTA-dianhydride. The copolymer with a graft ratio of 79% exhibited a good buffering capacity and pH sensitivity. These are attributed to protonation,deprotonation of the imidazole ring at around pH 7. The copolymers with less imidazole content did not show any apparent responses to changes in pH. The particle size of the copolymer aggregate formed under basic conditions was around 200,nm and increased with decreasing pH. The critical aggregation values at pH 6.0 and 8.0, derived from the changes of intensity ratios (I1/I3) in the emission spectrums of pyrene, were approximately 0.17 and 0.05,mg/ml, respectively. The surface charge of the aggregates increased with the decreasing pH as a result of the increase in protonation of imidazole and the tertiary amine in the polymer chain. The microviscosity of hydrophobic domains was estimated using 1,6-diphenyl-1,3,5-hexatriene. The decrease of the anisotropy value under acidic conditions reflects a disruption of hydrophobic interaction. Copyright © 2008 John Wiley & Sons, Ltd. [source] Limitation of immunoaffinity column for the removal of abundant proteins from plasma in quantitative plasma proteomicsBIOMEDICAL CHROMATOGRAPHY, Issue 5 2009Tomoko Ichibangase Abstract In plasma proteomics, before a proteome analysis, it is essential to prepare protein samples without high-abundance proteins, including albumin, via specific preparation techniques, such as immunoaffinity capture. However, our preliminary experiments suggested that functional changes with use alter the ability of the immunoaffinity column. Thus, in this study, to evaluate the changes of the removal ability of abundant proteins from plasma by the immunoaffinity column, plasma proteome analysis was performed for the long-term test for the reproducibility of the affinity column using the fluorogenic derivatization,liquid chromatography,tandem mass spectrometry method combined with an IgY column. The specific adsorption for albumin decreased with an increase in the number of the column usage before its expiration date. Moreover, it was demonstrated that hydrophobic high molecular weight compounds in plasma adsorbed onto the column materials surface contributed to the functional changes from specific immunoaffinity adsorption into hydrophobic interaction. These results suggested that, in quantitative plasma proteomics studies, it is important to keep in mind the risk of not only the nonselective loss but also the changes in the adsorption ability of the immunoafinity column. Copyright © 2008 John Wiley & Sons, Ltd. [source] Role of hydrophobic effect in the salt-induced dimerization of bovine ,-lactoglobulin at pH 3,BIOPOLYMERS, Issue 12 2009Giuseppe Graziano Abstract ,-Lactoglobulin is a dimeric protein around neutral pH, but the monomer becomes the dominant species at pH 3.0 due to strong electrostatic repulsions between the positively charged molecules. It has been found that the addition of salts to water at pH 3.0 favors the dimerization of ,-lactoglobulin. In particular, the dimer is the dominant species at 1M NaCl, 1M GuHCl, and 25 mM NaClO4 [Sakurai, Oobatake, and Goto, Protein Sci 2001, 10, 2325,2335]. The effect of these salt conditions on the strength of hydrophobic interaction has been calculated by means of a simple but physically sound approach. The obtained estimates indicate that: (a) the hydrophobic interaction contribution is strengthened in 1M NaCl and 1M GuHCl with respect to pure water, but not in 25 mM NaClO4; (b) anion binding on the positively charged surface of protein molecules has to be the major factor for the salt-induced dimerization. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 1182,1188, 2009. This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source] Mutation of residues critical for benzohydroxamic acid binding to horseradish peroxidase isoenzyme CBIOPOLYMERS, Issue 5 2001Barry D. Howes Abstract Aromatic substrate binding to peroxidases is mediated through hydrophobic and hydrogen bonding interactions between residues on the distal side of the heme and the substrate molecule. The effects of perturbing these interactions are investigated by an electronic absorption and resonance Raman study of benzohydroxamic acid (BHA) binding to a series of mutants of horseradish peroxidase isoenzyme C (HRPC). In particular, the Phe179 , Ala, His42 , Glu variants and the double mutant His42 , Glu:Arg38 , Leu are studied in their ferric state at pH 7 with and without BHA. A comparison of the data with those previously reported for wild-type HRPC and other distal site mutants reaffirms that in the resting state mutation of His42 leads to an increase of 6-coordinate aquo heme forms at the expense of the 5-coordinate heme state, which is the dominant species in wild-type HRPC. The His42Glu:Arg38Leu double mutant displays an enhanced proportion of the pentacoordinate heme state, similar to the single Arg38Leu mutant. The heme spin states are insensitive to mutation of the Phe179 residue. The BHA complexes of all mutants are found to have a greater amount of unbound form compared to the wild-type HRPC complex. It is apparent from the spectral changes induced on complexation with BHA that, although Phe179 provides an important hydrophobic interaction with BHA, the hydrogen bonds formed between His42 and, in particular, Arg38 and BHA assume a more critical role in the binding of BHA to the resting state. © 2001 John Wiley & Sons, Inc. Biopolymers (Biospectroscopy) 62: 261,267, 2001 [source] ,-Galactosidase from Lactobacillus pentosus: Purification, characterization and formation of galacto-oligosaccharidesBIOTECHNOLOGY JOURNAL, Issue 8 2010Thomas Maischberger Abstract A novel heterodimeric ,-galactosidase with a molecular mass of 105 kDa was purified from crude cell extracts of the soil isolate Lactobacillus pentosus KUB-ST10-1 using ammonium sulphate fractionation followed by hydrophobic interaction and affinity chromatography. The electrophoretically homogenous enzyme has a specific activity of 97 UoNPG/mg protein. The Km, kcat and kcat/Km values for lactose and o -nitrophenyl-,-D-galactopyranoside (oNPG) were 38 mM, 20 s -1, 530 M -1·s -1 and 1.67 mM, 540 s -1, 325 000 M -1·s -1, respectively. The temperature optimum of ,-galactosidase activity was 60,65°C for a 10-min assay, which is considerably higher than the values reported for other lactobacillal ,-galactosidases. Mg2+ ions enhanced both activity and stability significantly. L. pentosus ,-galactosidase was used for the production of prebiotic galacto-oligosaccharides (GOS) from lactose. A maximum yield of 31% GOS of total sugars was obtained at 78% lactose conversion. The enzyme showed a strong preference for the formation of ,-(1,3) and ,-(1,6) linkages, and the main transgalactosylation products identified were the disaccharides ,-D-Galp -(1,6)- D -Glc, ,-D-Galp -(1,3)- D -Glc, ,- D -Galp -(1,6)- D -Gal, ,- D -Galp -(1,3)- D -Gal, and the trisaccharides ,- D -Galp -(1,3)- D -Lac, ,- D -Galp -(1,6)- D -Lac. [source] Role of Kinases in Neuronal FunctionBIOTECHNOLOGY JOURNAL, Issue 8 2007Article first published online: 7 AUG 200 Cover illustration: Role of Cdk5 in neuronal function. Crystal structure of indirubin-38-monoxime in complex with Cdk5/p25 [1]. The inhibitor binds in the ATP-binding pocket of the catalytic subunit, mainly through hydrophobic interaction and two hydrogen bonds with Leu83. Indirubin-38-monoxime is shown as a ball-and-stick model, and the molecular surface of Cdk5/p25 is coloured according to electrostatic potential, with blue and red representing positive and negative potential, respectively. The figure was created with the program GRASP [2]. Courtesy of Claudia Crovace, Aldo Tarricone and Andrea Musacchio. [source] | |||||||||||||||||||||||||||||||||||||||||||