The enthalpies of interaction of polyvinylbenzyltrimethylammonium hydroxide with amino acids in aqueous solutions

The enthalpies of interaction of polyvinylbenzyltrimethylammonium (PVTA) hydroxide with glycine, glutamic acid, and tyrosine anions were determined calorimetrically. The interaction of PVTA with amino acid anions was shown to be an exothermic process. The enthalpy of interaction depended on the nature and concentration of the amino acid. The reaction became less exothermic and the time of the establishment of equilibrium increased as the concentration of amino acids grew.     

氨基酸从水到尿素水溶液中的迁移焓研究

用微量量热法测定甘氨酸、L-丙氨酸、L-丝氨酸在水和尿素水溶液中的溶解焓, 计算得到氨基酸从水到尿素水溶液的迁移焓, 并根据水合结构相互作用模型予以讨论. 结果表明, 氨基酸两性离子与尿素分子的静电作用以及两性离子头部与尿素分子的结构相互作用对氨基酸迁移焓有负贡献, 氨基酸侧链与尿素分子的结构相互作用依其亲水性或疏水性分别对迁移焓有负贡献或正贡献. 在实验浓度范围(0～13 mol/kg)内, 三种氨基酸的迁移焓总体上随尿素浓度的增加而下降, 其大小依次为L-丝氨酸＜甘氨酸＜L-丙氨酸, 氨基酸迁移焓的差异反映了溶质-溶剂结构相互作用的变化.     

Equivalent Electroconductivities of Lysine Cations and Phenylalanine Anions in Ionites KU-2-8 and AV-17

Equivalent conductivities of lysine cations and phenylalanine anions in ion-exchangers KU-2-8 and AV-17, respectively, are studied. The mobility of ions of amino acids in the ionites is lower than that of mineral ions (sodium and chloride). The obtained results are applied to predict the occurrence of electrochemical regeneration of ion-exchangers in the amino acid forms.     

Hydrophobic contribution of amino acids in peptides measured by hydrophobic interaction chromatography

The adsorption behaviors of amino acids in short chain peptides were examined. Each amino acid, aliphatic or charged, was inserted between the two tryptophans of a peptide, GWWG. The capacity factors of these peptides on an Ocytl-Sepharose column were measured. The adsorption enthalpies, entropies, and the number of repelled water molecules after adsorption were estimated to analyze the contribution of each different amino acid to its hydrophobic adsorption. The peptides inserted with aliphatic amino acids owned the highest capacity factors but released the least amount of adsorption heat among all the peptides under examination. It was found that the hydrophobic contribution of aliphatic amino acids was derived from the entropy gain by repelling the ordered water surrounding them. The insertion of negatively charged amino acids greatly reduced the capacity factors but still repelled a significant number of water molecules after adsorption. This indicated that the water molecules surrounding ionic amino acids were not orderly aligned. The dehydration cost energy but the water repelling did not offer enough entropy to drive the adsorption. Subsequently, lower retention was obtained from the peptides inserted with negatively charged ionic amino acids. The insertion of lysine increased the adsorption enthalpy but repelled no water molecules after adsorption. It was speculated that the inserted lysine still interacted with hydrophobic ligands but disturbed the interaction between ligands and adjacent tryptophans. Therefore, the adsorption enthalpy increased and the capacity factors decreased. Different amino acids contributed to hydrophobic interaction in different ways. The simultaneous analysis of capacity factor, adsorption enthalpy, adsorption entropy, and the number of repelled water molecules facilitated the understanding of the adsorption processes.     

Thermodynamics of the ionization of four difluorobenzoic and pentafluorobenzoic acids in water

Precision conductance measurements as a function of concentration and temperature between 0 and 100°C have been made for 2,3-, 2,5-, 3,4-, and 3,5-difluorobenzoic acids and pentafluorobenzoic acid in water. Standard state changes in enthalpy, entropy, and heat capacity as a function of temperature are reported for the ionization of these acids. Comparisons are made with other fluorobenzoic acids that have been reported earlier and with the corresponding methylbenzoic acids. The differences between the ionization of a fluorobenzoic acid and its counterpart methylbenzoic acid is almost entirely a difference in the entropies of ionization with only a small difference in the enthalpies of ionization. Each fluorine substituted in the meta or para position increases the entropy of ionization while substitution in the ortho position decreases the entropy. This is in contrast to the effect of methyl substitution where substitution in any position decreases the entropy of ionization. Walden products for the various anions follow the pattern found for the methylbenzoate anions with a sharp increase from 0 to about 30°C and with ortho substituted anions less mobile than those without ortho substitutents.     

Heats of Mixing of Aqueous Solutions of Alkali Metal Salts of Substituted Benzenesulfonic Acids

The enthalpy change on mixing aqueous solutions of substituted benzene sulfonic acids and their salts, with salts having a common cation or anion, were measured at constant total ionic strength and at 25°C. The results are qualitatively interpreted in terms of solute–water structural properties and the ion size effect. The heat effects of mixing solutions having common anions obey the sign rule of Young and Smith. In anion–common cation mixings at concentration of 0.5 mol-kg^–1 only exothermic heat effects were observed, whose magnitude increase with the increasing difference in size of the mixed anions. The magnitude of the mixing effect increased with the salt concentration in cation–common anion mixing processes, In anion–common cation mixings the enthalpy of mixing changes sign from negative to positive, indicating a predominantly endothermic effect as concentration increases.     

Stabilization of zwitterionic structures of amino acids (Gly, Ala, Val, Leu, Ile, Ser and Pro) by ammonium ions in the gas phase

The thermochemistry of gas-phase ion-molecule interactions and structures of a variety of clusters formed between protonated amino acids and either ammonia or amines have been studied by pulsed ionization high-pressure mass spectrometry (HPMS) and ab initio calculations. The enthalpy changes for the association reactions of protonated Gly, Ala, Val, Leu, Ile, Ser, and Pro with ammonia have been measured as -23.2, -21.9, -21.0, -20.8, -20.6, -22.6, and -20.4 kcal mol(-1), respectively. A very good linear relationship exists between the enthalpy changes and the proton affinities (PAs) of the amino acids, with an exception of Ser, where the hydroxyl substituent forms an extra hydrogen bond with ammonia. For the association reaction of protonated proline and methylamine, the measured enthalpy and entropy changes are -26.6 kcal mol(-1) and -30.1 cal mol(-1) K(-1), respectively. The experimental and calculated results indicate that the zwitterionic structure of proline may be well stabilized by CH3NH3(+). For the first time, the interaction strengths between these amino acids and NH4(+) have been obtained, and comparison with Na+ is discussed. Stabilization of zwitterionic structures of a series of amino acids (Gly, Ala, Val, Ser, and Pro) by various ammonium ions (NH4(+), CH3NH3(+), (CH3)2NH2(+), and (CH3)3NH+) has been investigated systematically. Energy decomposition analysis has been performed so that the salt bridge interaction strengths between zwitterionic amino acids and ammonium ions have been obtained. Some generalizations with respect to the relative stability of zwitterionic structures may be drawn. First, as the PA of an amino acid increases, within a series of Gly, Ala, Val, the zwitterionic structure becomes more energetically favorable relative to a non-zwitterionic isomer. Second, as the PA of an amine increases, the zwitterionic structure of a given amino acid within the complex becomes gradually less favorable. Third, compared to the other amino acids, Pro, the only secondary amine among the 20 naturally occurring amino acids, has a much more pronounced tendency to form the zwitterionic structure, which has been confirmed by the experimental results. Finally, substituents on the amino acid backbone that may participate in additional hydrogen bond interactions in non-zwitterionic isomer may render it more stable, as seen in Ser. These organic ammonium ions are found to be able to very effectively stabilize the zwitterionic structure of amino acids, even more effectively than metal ions, which aids significantly in the understanding of why zwitterionic structures exist extensively in biological systems.     

Study of mixed micellar aqueous solutions of sodium dodecyl sulfate and amino acids

Thermodynamic properties of sodium dodecyl sulfate (SDS) in micellar aqueous solutions of L-serine and L-threonine were determined by fluorescence spectroscopy and dynamic light scattering techniques. The values of Gibbs free energy, enthalpy and entropy of the process of micelle formation were calculated using the critical micelle concentration and degree of dissociation. Changes in critical micelle concentration of SDS with the addition of amino acids were examined by both conductivity and pyrene I ₁/I ₃ ratio methods at different temperatures. The pyrene fluorescence spectra were used to study the change of micropolarity produced by the interaction of SDS with amino acids. The aggregation behavior of SDS was explained in terms of structural changes in mixed solutions. The data on dynamic light scattering suggest that size of SDS micelles was influenced by the presence of amino acids.     

基于吸附质-分子探针的阴离子聚合物微球吸附性能研究

制备了SO42-、NO3-、ClO4-和F-、Cl-、Br-、I-两种新型阴离子苯乙烯-二乙烯苯聚合物微球,基于吸附质-分子探针电导法,研究了阴离子聚合物吸附低浓度游离酸的性能,考察了阴离子类型和温度对吸附行为的影响。实验结果表明,在30℃时,吸附游离酸的过程,遵循单分子层机理进行吸附。吸附剂-吸附质相互作用能U制约表观吸附速率常数K,两者存在线性相关性,K、U均随阴离子的离子势增大呈逐渐减小的趋势。吸附过程为吸热的,吸附焓变ΔH为10.87 kJ.mol-1。吸附过程谱维数ds增大,导致表观吸附速率常数降低。吸附质对吸附剂的亲和能Ua随吸附质-吸附剂相互作用参数K2增大而减小。     

Enthalpies of Anion Exchange of Chloride by Pyridinecarboxylate in AV-17-8 Anionite

Russian Journal of Physical Chemistry A - Enthalpies of Cl– anion exchange for anions of nicotinic, isonicotinic, dipicolinic, and cinchomeronic acids on the strongly basic anionite AV-17-8...     

Ionization of five aqueous fluorobenzoic acids: Conductance and thermodynamics

The three monofluorobenzoic acids together with 2,4-difluoro and 2,6-difluorobenzoic acids in aqueous solution are the subject of precision conductance measurements. The experimental data are analyzed to give ionization constants and limiting conductances at temperatures from 0 to 100°C. Walden products for the acid anions are derived from the limiting conductances while the ionization consatants are fitted by statistical methods to the function pK _a (m)=A+B/T+ C logT+DT. Only the 2,6- acid requires the fourth term of the function to fit the data to a precision of better than 0.03%. Mathematical analysis of the pK function gives the standard changes in enthalpy, entropy, and heat capacity. All the acids studied are more acidic than the parent, benzoic acid, as well as more acidic than the isoelectronic methylbenzoic acids. In general the increased acidity is tied to decreases in enthalpy while entropy changes on ionization differn little from those found for the parent acid.     

Computer simulation of amino acid sorption on carbon nanotubes

A computer simulation of complexes of (6,6) open carbon nanotubes (CNTs) with neutral molecules, zwitterions and glycine, alanine, and phenylalanine amino acid anions is performed. In starting structures amino acids are arranged in three types: on the external side face, the open end, and inside CNT. The structure is optimized within the density functional theory with regard to the GD3 dispersion correction with and without taking into account solvation effects. It is found that the greatest CNT–amino acid interaction occurs in the neutral aqueous medium at dissociative chemisorption of the zwitterion (adsorption energy 80-90 kcal/mol) and in the basic medium at anion chemisorption (energy ~48-50 kcal/mol) on the open CNT end.     

Thermodynamical characteristics of the reaction of pyridoxal-5′-phosphate with L-amino acids in aqueous buffer solution

The reaction of pyridoxal-5′-phosphate with L-isomers of alanine, lysine, arginine, aspartic acid, glutamic acid, and glycine in phosphate buffer solution was studied by absorption spectroscopy and the calorimetry of dissolution at physiological acidity of the medium (pH 7.35). The formation constants of Schiff bases during reactions and changes in Gibbs energy, enthalpy, and entropy were determined. It was shown that the formation constant of the Schiff base and its spectral properties depend on the nature of the bound amino acid. The progress of the reaction with a majority of amino acids is governed by the entropy factor due to the predominant role of the dehydration effect of the reaction center of amino acids during chemical reactions. The intramolecular electrostatic interaction of an ionized phosphate group with the positively charged amino group on the end of the chain of amino acid residue stabilizes the Schiff bases formed by lysine and arginine. The extinction coefficient of the base, equilibrium constant, and the exothermic effect of the reaction then increase. The excess negative charge on the end of the chain of amino acid residues of aspartic and glutamic acids destabilizes the molecule of the Schiff base. In this case, the equilibrium constant decreases and the endothermic effect of the reaction increases.     

Study on physicochemical properties of ionic liquids based on alanine [Cnmim][Ala] (N=2,3,4,5,6)

According to Fukumoto's method, a new series of ionic liquids (ILs) based on alanine, [Cnmim][Ala] ( n=2,3,4,5,6), which comprise 1-alkyl-3-methylimidazolium cation ([Cnmim](+)) and alanine anions ([Ala] (-)), were prepared and characterized. In terms of standard addition method, the density and surface tension of amino acid ILs [Cnmim][Ala] (1-alkyl-3-methylimidazolium alpha-aminopropionic acid salt) were measured in the temperature range 293.15-343.15+/-0.05 K. The volume and surface properties of the ILs [Cnmim][Ala] were discussed. A new method of determining parachor of ionic compound was proposed and was applied to estimate the physicochemical properties of amino acid ionic liquids (AAILs): molecular volume, surface tension, molar enthalpy of vaporization, and thermal expansion coefficient. In comparison with Deetlefs's method of using neutral parachor contribution, the method proposed in this work makes smaller error in estimating properties of AAILs.     

Anionic Lead Complexes on the Solid Phase of Fibrous Filled Materials in the Reaction with 4(2-Pyridylazo)resorcinol

The influence of the nature of anions (iodide, bromide, thiosulfate, pyrophosphate, tartrate, and acetate) in the anionic lead complex adsorbed on a solid phase of a fibrous sorbent filled with the AV-17 anion exchanger on the color reaction between lead and 4-(2-pyridylazo)resorcinol (PAR) was studied by diffuse reflectance spectrometry. The influence of anions on the complexation of lead with PAR on the solid phase was discussed for different types of the color reaction. It was demonstrated that the reactions with iodide at pH 5–10 and with thiosulfate at pH 10 are significant in the determination of lead as three-component complexes on the support. In the presence of other anions, lead ions do not react with PAR on the AV-17 solid phase.     

脂肪族α-氨基酸疏水自缔合作用的流动微量热法研究

建立了水溶液中脂肪族α- 氨基酸疏水自缔合相互作用的化学模型, 根据模型方程对由精密流动微量热法测得的α- 氨基酸水溶液的稀释焓数据进行回归分析, 得到等步自缔合作用的平衡常数(K)、焓变(ΔHm)和熵变(ΔSm)等热力学参数, 发现焓、熵之间存在很好的补偿关系. 同时计算了溶液中水的偏摩尔过量熵(SE1), 并根据脂肪族α- 氨基酸的水化模型对结果进行了讨论. 建立的化学模型参数能在一定程度上解释McMillan- Mayer模型中的同系焓作用系数的物理意义.     

Enthalpic pair interaction coefficient between zwitterions of L-alpha-amino acids and urea molecule as a hydrophobicity parameter of amino acid side chains

Dissolution enthalpies of L-alpha-proline, L-alpha-tyrosine, L-alpha-tryptophan, L-alpha-histidyne, L-alpha-arginine, L-alpha-lysine, L-aspartic acid, and L-alpha-glutamic acid in aqueous solutions of urea have been measured by calorimetry at a temperature of 298.15 K. The values of dissolution enthalpy were used to determine enthalpic heterogeneous pair interaction coefficients between the zwitterions of the natural amino acids and a molecule of urea in water solution. These coefficients were interpreted in terms of the hydrophobic or hydrophilic effects of the side chains of amino acids on their interactions with a polar molecule of urea in water.     

Thermodynamics of hydrophobic interaction chromatography of acetyl amino acid methyl esters

Thermodynamic analysis of hydrophobic interaction chromatography of amino acid methyl esters showed entropy-driven adsorption, consistent with solvophobic theory, except for phenyl ester on the Toyopearl resins. All esters adsorbed more strongly to the Toyopearl resins, including the polymethacrylate base matrix, than to Butyl Sepharose. Enthalpy changes were more favorable with the former, explaining the retention difference between Toyopearl Butyl and Butyl Sepharose. An enthalpy change versus heat capacity change plot showed Van der Waals interactions predominantly with the resin matrix. Literature data revealed the same effect for dansylamino acids, shown by isothermodynamic temperature analysis to adsorb more entropically than the esters.     

Enthalpy changes upon dilution and ionization of poly(L-glutamic acid) in aqueous solutions

The enthalpy changes accompanying the dilution and ionization of poly(L-glutamic acid) in water have been measured at 25 degrees C for two degrees of polymerization (DP = 115 and DP = 480) at various degrees of ionization, alpha, for a concentration range from about 0.2 to 0.002 monomol/L. The heat of dilution displays an unusual dependence on the degree of ionization, which is in sharp contrast to the behavior of other weak carboxylic polyelectrolytes, such as poly(acrylic acid). The exothermic heat effects observed at low values of alpha become endothermic for the region where the helix-coil transition is most pronounced, and for high degrees of ionization, they are exothermic again. Evidently, an endothermic heat effect, produced by an additional conformational transition in the dilution process, is superimposed on the exothermic enthalpy of dilution, and it overweighs the latter in the region of alpha where the conformational transition is prevailing. The calorimetric titration curve, which gives the dependence of the heat of ionization, deltaH(i), on alpha, has a maximum and is typical for poly(carboxylic acids) which undergo pH-induced conformational transition, such as poly(methacrylic acid). The values of deltaH(i) obtained at two polymer concentrations indicate that the enthalpy of ionization depends on the polypeptide concentration.     

Correlation analysis of substituent effects on the acidity of benzoic acids by the AM1 method

Theoretical analysis of the electronic effect of aromatic substituents was done with the use of the AM1 computational procedure. The gas-phase acidity of substituted benzoic acids was linear with the difference in the heat of formation between corresponding benzoic acids and benzoate anions, the energy of the highest occupied molecular orbital, and the net charge on the acidic oxygen atoms of the corresponding benzoate anions. The Hammett σ constant was linearly correlated with the net charge on the atoms of the acid moiety of substituted benzoic acids. The AM1 computational procedure satisfactorily reproduced the electronic properties of a wide variety of substituents.