Densities and Speeds of Sound of Antibiotic Drug Chloramphenicol

Article pubs.acs.org/jced

Densities and Speeds of Sound of Antibiotic Drug Chloramphenicol with L‑Leucine and Glycyl‑L‑leucine in Aqueous Medium at T = (288.15−318.15) K: A Volumetric, Ultrasonic, and UV Absorption Study Harsh Kumar* and Isha Behal Department of Chemistry, Dr. B. R. Ambedkar National Institute of Technology, Jalandhar 144011, Punjab, India S Supporting Information *

ABSTRACT: From the density (ρ) and speed of sound (c) measurements, the interactions of drug chloramphenicol with L-leucine and the dipeptide glycyl-L-leucine, have been examined in aqueous medium at T = (288.15−318.15) K and experimental pressure p = 0.1 MPa. For L-leucine and the dipeptide, the apparent molar volume (Vϕ), the apparent partial molar volume (Voϕ), and the apparent partial molar volumes of transfer (ΔV ϕo ), from water to aqueous chloramphenicol have been calculated from density data. We have also calculated the limiting apparent molar expansibilities. From the speed of sound data, apparent molar isentropic compression (K ϕ,s ), apparent partial molar isentropic compression (Koϕ,s), and apparent partial molar isentropic compression of transfer (ΔKoϕ,s) have been calculated. The pair and triplet interaction coefficients are determined from apparent partial molar volumes of transfer and apparent partial molar isentropic compression of transfer. For the present mixtures, the absorption spectra have also been recorded with the help of UV−visible spectrophotometer. Through the perusal of these calculated parameters, a detailed insight into the physicochemical interactions, for example, ion−hydrophilic, hydrophilic− hydrophilic, and hydrophilic−hydrophobic interactions in the L-leucine/glycyl-L-leucine-drug system, along with the structuremaking/structure-breaking tendency of the L-leucine and the dipeptide, have been obtained. solutes.11−15 For a better understanding of these molecules in the medium, it is necessary to determine the state and functionality of the molecules in the medium.16,17 To better illuminate these phenomena, several building blocks and model compounds of proteins (like amino acids/peptides) having low molar mass have been analyzed because it is not feasible to have direct thermodynamics studies on three-dimensional proteins having complex conformations. The insight about the functioning of proteins, their structure, and conformation changes18 in aqueous solutions is provided by the solute− solvent interactions between the side chain of the amino acid/ backbone and peptide, which act as solute and solvent molecules. Model compounds like amino acids have attracted significant interest because side chains of amino acids and peptide chains contribute toward the magnitude and type of interactions, and furthermore, the structure of these model compounds can be easily transformed. Various researchers19−26 have investigated solute−solvent interactions of these model compounds in aqueous and mixed aqueous solutions by

1. INTRODUCTION In all the metabolic pathways or biological processes occurring inside the body, the drug−protein interactions have an important role. Modern drug discovery is dependent upon these interactions to reveal target proteins which are responsible for the pharmacological action by biological molecules.1,2A lot of interest have been evoked by the recognition of drugs activities in aqueous and nonaqueous solutions, which involve the interactions with biological membranes.3−7 Physiologically, the consequences of a drug’s action such as movement of the drug through the bloodstream, distributions, receptor binding, and lastly, desired actions involve an intricate mechanism8 which can be perceived by knowing the thermodynamic behavior of such systems indicated by different noncovalent interactions. The stabilization of the native conformation of biological molecules (proteins) are associated with several noncovalent interactions encompassing hydrogen-bonding, electrostatic, and hydrophobic interactions.9,10The properties such as solubility, hydration, and enzyme activity for the globular proteins are effected due to changes in water structure and solute−solvent interactions in the presence of solute; hydration, solubility, and the activity of enzymes are affected by the presence of these © 2016 American Chemical Society

Received: February 25, 2016 Accepted: October 12, 2016 Published: October 24, 2016 3740

DOI: 10.1021/acs.jced.6b00168 J. Chem. Eng. Data 2016, 61, 3740−3751

Journal of Chemical & Engineering Data

Article

Table 1. Specification of Studied Chemicals

a

Declared by the supplier.

CPA 225D balance having precision of ±0.00001 g) as per details given earlier28 have been made using the Anton Paar DSA 5000 M densimeter. The calibration and other procedures have been given in our earlier paper.28 The speed of sound measurements were carried out at a frequency of 3 MHz. The density and speeds of sound values are extremely sensitive to temperature, so it was controlled to ±1 × 10−3 K by a built-in Peltier device. The sensitivity of the instrument corresponds to a precision in density and speeds of sound measurements of 1 × 10−3 kg m−3 and 1 × 10−2 m·s−1. The standard uncertainty of the density and speed of sound are 0.05 kg m−3 and 0.5 ms−1, respectively.

determining the different physicochemical parameters. Studies on aqueous solutions of amino acid/drug and peptide/drug are essential to understand the chemistry behind the biological systems. Thus, analysis of drug−protein interactions has become an important issue for drug development and its efficacy.27 Despite the significant importance of field, few studies on physicochemical properties aqueous amino acids + drug mixtures have been reported so far.28−32 Therefore, we decided to carry out the volumetric and acoustic studies of Lleucine and the dipeptide glycyl-L-leucine in an aqueous solution of antibiotic drug chloramphenicol in order to have a better understanding about the interactions in the present mixtures. The antibiotic drug chloramphenicol (C11H12Cl2N2O5) is used for the treatment of of bacterial infections like plague, cholera, and meningitis, and it is also used against other significant infections like typhoid fever. Here, in this paper, the densities and speed of sound of L-leucine and glycyl-L-leucine in aqueous chloramphenicol solutions at T = (288.15−318.15) K and experimental pressure p = 0.1 MPa have been reported. We have also recorded the absorption spectra using UV−visible spectrophotometer for mixtures used in this study. Density and speed of sound data have been used to determine the apparent molar parameters. These determined parameters have been discussed to interpret solute−solute and solvent−solvent interactions and also to have insight about the structuremaking and structure-breaking capability of solute (i.e., amino acids/dipeptide molecules).

3. RESULTS AND DISCUSSION 3.1. Volumetric Properties. 3.1.1. Apparent Molar Volume. Densities (ρ) of L-leucine and the dipeptide glycyl-Lleucine in (0.000, 0.0005, 0.001, 0.002, and 0.004) mol·kg−1 aqueous chloramphenicol solutions measured at T = (288.15, 298.15, 308.15, and 318.15) K are reported in Table 2. The experimental density values in the case of aqueous L-leucine solutions and aqueous glycyl-L-leucine solutions at different temperatures are in good agreement with literature density values33−36 compared in this paper. The comparison has been graphically shown in Figures 1 and 2, in which density values follow the sequence with temperature. From the Figures 1and 2, it is observed that experimental densities for the mixture under study shows the same trend as literature densities; that is, density values follow the sequence with reference to temperature, which means that density values decrease with an increase in temperature. The apparent molar volumes (Vϕ) are calculated with experimental density values using equation:

2. EXPERIMENTAL SECTION 2.1. Materials. L-Leucine with mass fraction purity ≥0.99 procured from Merck, Germany, was used as received. Glycyl-Lleucine and chloramphenicol with mass fraction purity≥ 0.98 and ≥0.97, respectively, were purchased from HiMedia Laboratories Pvt. Ltd., India, and used as received. The chemicals used in the present study were vacuum-dried over P2O5 in a desiccator for 48 h to avoid contamination due to moisture absorption. The specifications of the chemicals used in this study are also given in Table 1. 2.2. Apparatus and Procedure. Density and speed of sound measurement of the samples prepared (using Sartorius

Vϕ = M /ρ − (ρ − ρο )/mA ρρο

(1) −1

where M is the molar mass of the solute (kg·mol ), mA is the molality (mol·kg−1) of the amino acid or dipeptide, that is, the amount of solute (amino acid or dipeptide) per one kilogram of solvent (mixture of water + chloramphenicol), and ρo and ρ are the densities (kg·m−3) of the solvent and solution, respectively. The apparent molar volumes along with density values are reported in Table 2. The estimate of uncertainty values for Vϕ are ± (0.05−0.007) × 106 m3·mol−1. Strong solute−solvent 3741



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Table 2. Values of Densities, ρ, and Apparent Molar Volumes, Vϕ of L-leucine and Glycyl-L-leucine in Aqueous Solutions of Chloramphenicol at Different Temperatures and Experimental Pressure, p = 0.1 MPa ρ × 103 (kg·m−3) mAa

−1

(mol·kg )

T = 288.15 K

T = 298.15 K

T = 308.15 K

Vϕ × 106 (m3·mol−1) T = 318.15 K

T = 288.15 K

T = 298.15 K

T = 308.15 K

T = 318.15 K

107.38 107.72 107.65 107.59 107.82 107.71 107.61 107.72

109.26 108.22 108.30 108.52 108.59 108.59 108.59 108.76

110.11 110.09 110.04 109.99 109.94 109.89 109.83 109.77

112.35 111.04 109.38 108.64 108.60 108.36 108.15 107.84

112.74 111.52 109.99 109.56 109.56 109.47 109.18 109.00

113.00 113.32 111.56 111.11 110.66 110.63 110.16 109.78

112.90 111.78 110.39 109.11 108.93 108.68 108.36 107.88

112.70 112.31 110.79 110.23 109.99 109.79 109.45 109.16

113.37 113.57 112.21 111.54 110.84 110.56 110.23 109.81

113.10 112.92 110.79 109.44 109.01 108.83 108.54 108.22

113.58 114.61 112.06 110.28 109.85 109.68 109.41 109.11

113.96 114.99 112.73 111.27 110.55 110.40 110.36 109.89

115.41 113.29 110.76 109.65 108.88 108.85 108.60 108.59

116.95 113.78 111.16 110.22 109.54 109.57 109.33 109.37

117.88 114.71 112.52 111.41 111.00 110.61 110.36 110.36

140.94 138.47 138.32 139.10 139.43 139.15

140.73 140.22 140.11 140.39 140.76 140.49

141.09 142.23 141.58 142.09 142.38 141.99

−1

0.00000b 0.00991 0.02042 0.04026 0.06014 0.08020 0.10017 0.12459 0.15022

0.999119b 0.999363 0.999615 1.000092 1.000598 1.001067 1.001567 1.002135 1.002712

0.997052b 0.997290 0.997535 0.998005 0.998476 0.998929 0.999402 0.999979 1.000556

0.00000b 0.01007 0.01971 0.04149 0.06003 0.08062 0.09922 0.12447 0.14973

0.999273b 0.999458 0.999681 1.000197 1.000682 1.001143 1.001616 1.002192 1.002772

0.997209b 0.997403 0.997610 0.998119 0.998567 0.999032 0.999472 1.000066 1.000682

0.00000b 0.01017 0.02021 0.03985 0.05986 0.08035 0.09955 0.12465 0.14942

0.999429b 0.999612 0.999833 1.000284 1.000773 1.001283 1.001735 1.002346 1.002942

0.997363b 0.997536 0.997759 0.998197 0.998689 0.999153 0.999601 1.000196 1.000821

0.00000b 0.01045 0.02017 0.04036 0.06051 0.08038 0.10071 0.12607 0.15125

0.999643b 0.999818 1.000014 1.000486 1.001013 1.001494 1.001976 1.002592 1.003213

0.997576b 0.997767 0.997948 0.998404 0.998895 0.999359 0.999823 1.000417 1.001022

0.00000b 0.01039 0.02044 0.04027 0.06032 0.08028 0.10003 0.12525 0.15016

0.999922b 1.000094 1.000290 1.000783 1.001276 1.001778 1.002242 1.002856 1.003432

0.997847b 0.997993 0.998199 0.998675 0.999152 0.999638 1.000089 1.000678 1.001235

0.00000b 0.01036 0.02041 0.04005 0.06009 0.08023 0.09965

0.999119b 0.999623 1.000139 1.00113 1.002126 1.003078 1.004024

0.997052b 0.997544 0.99807 0.99905 0.999995 1.000945 1.001902

L-leucine + 0.0000 mol·kg chloramphenicol 0.994047b 0.990216b 0.994279 0.990433 106.60 0.994535 0.990663 106.90 0.994994 0.991098 106.97 0.995441 0.991533 106.50 0.995893 0.991972 106.76 0.996345 0.992410 106.55 0.996896 0.992945 106.72 0.997446 0.993506 106.94 −1 L-leucine + 0.0005 mol·kg chloramphenicol 0.994205b 0.990372b 0.994379 0.990551 112.15 0.994602 0.990741 110.49 0.995101 0.991218 108.87 0.995524 0.991620 107.61 0.995973 0.992080 107.84 0.996385 0.992473 107.37 0.996968 0.993057 107.47 0.997546 0.993648 107.49 −1 L-leucine + 0.001 mol·kg chloramphenicol 0.994356b 0.990522b 0.994549 0.990695 112.21 0.994747 0.990895 111.19 0.995185 0.991309 109.67 0.995631 0.991741 108.62 0.996083 0.992209 107.95 0.996511 0.992635 107.81 0.997088 0.993200 107.51 0.997665 0.993785 107.33 −1 L-leucine + 0.002 mol·kg chloramphenicol 0.994560b 0.990713b 0.994747 0.990906 112.44 0.994954 0.991067 112.77 0.995378 0.991499 110.23 0.995845 0.991960 108.41 0.996297 0.992422 107.98 0.996749 0.992864 107.79 0.997325 0.993404 107.49 0.997913 0.994001 107.22 −1 L-leucine + 0.004 mol·kg chloramphenicol 0.994831b 0.990992b 0.994985 0.991161 114.70 0.995191 0.991341 112.89 0.995654 0.991775 109.75 0.996118 0.992229 108.66 0.996591 0.992664 107.89 0.997028 0.993120 107.89 0.997603 0.993680 107.59 0.998142 0.994207 107.60 glycyl-L-leucine + 0.0000 mol·kg−1chloramphenicol 0.994047b 0.990216b 0.994554 0.990713 139.59 0.995045 0.991171 138.19 0.995995 0.99211 137.81 0.99694 0.99302 137.85 0.997866 0.993927 138.41 0.998802 0.99485 138.40

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Table 2. continued ρ × 103 (kg·m−3) mAa (mol·kg−1)

T = 288.15 K

T = 298.15 K

0.15021 0.20139

1.006404 1.008794

1.004282 1.006662

0.00000b 0.01036 0.02032 0.04039 0.06034 0.08022 0.09911 0.14913 0.19989

0.999273b 0.999769 1.000283 1.001275 1.002231 1.003206 1.004121 1.006466 1.008847

0.997209b 0.9977 0.998217 0.999211 1.000149 1.001114 1.002015 1.004363 1.006753

0.00000b 0.01019 0.02032 0.03986 0.05971 0.07953 0.10031 0.14922 0.19968

0.999429b 0.999913 1.000426 1.001394 1.002376 1.003308 1.004348 1.006622 1.009025

0.997363b 0.997846 0.998349 0.99932 1.000274 1.00121 1.00222 1.004546 1.006886

0.00000b 0.01043 0.02013 0.04061 0.05996 0.08056 0.10002 0.14767 0.19921

0.999643b 1.000122 1.000580 1.001584 1.002553 1.003557 1.004497 1.006720 1.009157

0.997576b 0.998045 0.998515 0.999524 1.000478 1.001453 1.002357 1.004636 1.007004

0.00000b 0.00994 0.02025 0.04021 0.05997 0.08027 0.10009 0.14974 0.19934

0.999922b 1.000371 1.000844 1.001831 1.002818 1.003811 1.004737 1.007048 1.009417

0.997847b 0.998292 0.998769 0.999739 1.000697 1.001664 1.002582 1.004963 1.007260

T = 308.15 K

Vϕ × 106 (m3·mol−1) T = 318.15 K

T = 288.15 K

1.001187 0.997236 138.79 1.003567 0.99961 138.92 glycyl-L-leucine + 0.0005 mol·kg−1chloramphenicol 0.994205b 0.990372b 0.994697 0.990859 140.35 0.995192 0.991313 138.44 0.99614 0.992266 138.44 0.997091 0.993169 138.86 0.998024 0.994064 138.72 0.998933 0.994969 138.70 1.001291 0.997324 139.06 1.003639 0.999672 139.06 glycyl-L-leucine + 0.001 mol·kg−1chloramphenicol 0.994356b 0.990522b 0.994834 0.990972 140.71 0.995332 0.991449 139.07 0.996272 0.992354 138.71 0.997205 0.993271 138.51 0.998118 0.994167 138.96 0.999155 0.995137 138.56 1.001426 0.997456 139.07 1.003754 0.999805 138.89 glycyl-L-leucine + 0.002 mol·kg−1chloramphenicol 0.994560b 0.990713b 0.995028 0.991178 142.27 0.995504 0.991636 141.58 0.996498 0.992595 140.19 0.997416 0.993476 139.32 0.998370 0.994411 139.13 0.999314 0.995320 139.05 1.001531 0.997593 139.35 1.003905 0.999979 139.17 glycyl-L-leucine+ 0.004 mol·kg−1chloramphenicol 0.994831b 0.990992b 0.995276 0.991428 143.00 0.995743 0.991886 142.57 0.996711 0.992845 140.49 0.997649 0.993726 139.54 0.998592 0.994661 139.24 0.999549 0.995570 139.45 1.001876 0.997933 139.65 1.004183 1.000249 139.28

T = 298.15 K

T = 308.15 K

T = 318.15 K

139.35 139.44

140.31 140.22

141.42 141.17

141.02 138.73 138.63 139.34 139.25 139.32 139.51 139.40

141.21 140.04 140.58 140.53 140.62 140.39 140.25 140.24

142.06 142.70 141.97 142.39 142.60 142.11 141.53 141.29

141.00 139.80 139.09 139.30 139.56 139.37 139.33 139.45

141.78 140.58 140.41 140.63 140.92 140.23 140.38 140.36

143.64 143.39 142.92 142.70 142.79 142.47 141.67 141.32

143.43 141.67 140.21 139.64 139.78 139.98 139.65 139.80

143.82 141.71 140.73 140.70 140.90 140.53 140.54 140.51

144.50 143.14 142.50 142.64 142.69 142.40 141.54 141.28

143.60 142.77 141.11 140.50 140.34 140.45 139.90 139.89

143.90 143.56 141.69 141.32 141.33 140.91 140.67 140.48

145.21 144.85 142.74 143.12 142.86 142.70 141.74 141.33

a

mA is the molality of amino acid or its dipeptide in aqueous chloramphenicol solutions. bValues of densities taken from our earlier paper;64 standard uncertainties u are u(m) = 2 × 10−5 mol·kg−1, u(T) = 0.01 K, u (ρ) = 0.05 kg·m−3, and u (p) = 0.01 MPa.

interactions are indicated by the positive values of Vϕ. Also, the increase in Vϕ values with an increase in temperature results in greater affinity for the solvent which further suggest that the solute−solvent interactions are greatly enhanced. The higher values of apparent molar volume in glycyl-L-leucine as compared to L-leucine suggest more solute−solvent interactions in the case of glycyl-L-leucine than L-leucine, as shown in Scheme 1. 3.1.2. Apparent Partial Molar Volume. Apparent partial molar volume Voϕ, calculated using eq E1 of the Supporting Information by means of least-squares fit of Vϕ values. The values of Voϕ and SV* together with standard errors derived by least-squares fitting of the Vϕ values to eq E1 are reported in Table S1. Table S1 also reports the literature values37−43 of Voϕ

for aqueous L-leucine and glycyl-L-leucine. For L-leucine and the dipeptide glycyl-L-leucine, the positive Voϕ values, indicating the presence of solute−solvent interactions, increase with an increase in the chloramphenicol concentration and temperature. According to the cosphere overlap model,44,45 there is an increase in volume when the cospheres of two ionic species overlap, whereas volume decreases by an overlap of hydrophobic−hydrophobic groups and ion-hydrophobic groups. Ion−hydrophilic interactions are indicated by the observed positive Voϕ values, which dominate over ion−hydrophobic interactions and hydrophobic−hydrophobic interactions. Because solute−solute interactions like ion−ion or zwitterion− zwitterion interactions at infinite dilution are negligible, vital information on solute−solvent interactions is provided by 3743



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Figure 1. Plots of experimental and literature values (refs 33,34) of densities for (L-leucine + water) mixtures at different temperatures.

Figure 2. Plots of experimental and literature values (refs 35,36) of densities for (glycyl-L-leucine + water) mixtures at different temperatures.

the expansion of solution, suggests the larger values of Voϕ at higher temperatures. Moreover, the higher Voϕ values in the case of glycyl-L-leucine as compared to L-leucine suggest the increase in values of Voϕ with increase in the molar mass or peptide linkage and also suggest that solute−solvent interactions are enhanced in glycyl-L-leucine as compared to L-leucine. The magnitude of SV* is negative for all concentrations of chloramphenicol at all temperatures except for the aqueous solution of L-leucine as observed from Table S1. Weak solute−

temperature dependence of the apparent partial molar property. The Voϕ values increase with an increase in temperature for Lleucine and the dipeptide, which may be due to the fact that some solvation molecules are released from the loose solvation layers of the solutes in solution. It can be further described by taking in to the consideration of the size of solvation layers (primary as well as secondary) around zwitterions. The release of the solvent from the secondary solvation layers of amino acid zwitterions to the bulk solvent at higher temperature, leading to 3744



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theoretical Vϕo values were calculated. In Table S3, the deviations obtained from experimental Voϕ and theoretical Voϕ values are also reported. The eq E4 given in Supporting Information has been used to calculate the deviations, the values of which are very small indicating that the polynomial equation fits very well in the present study. By using the relation E5 of Supporting Information, the temperature dependence of apparent partial molar volume (Voϕ) can be expressed in terms of the absolute temperature (T). The limiting apparent molar expansibilities at infinite dilution, Eoϕ = (∂Voϕ/∂T)p is considered a useful measure49 of solute−solvent interactions prevailing in the solution. Hepler50 developed the general thermodynamic expression E6 of the Supporting Information for determining the structure maker or structure breaker characteristics of the solute. The sign of (∂Eoϕ/ ∂T)p50,51 suggests that structure making solutes have positive and small negative (∂Eϕo /∂T)p values, whereas structurebreaking solutes have negative (∂Eoϕ/∂T)p values. The Eoϕ and (∂Eoϕ/∂T)p values are reported in Table S4 of Supporting Information. Except for (glycyl-L-leucine + 0.001 mol·kg−1 chloramphenicol at 288.15K), the positive Eoϕ values have been found at all temperatures and concentrations of chloramphenicol. The presence of solute−solvent interactions in these systems is concluded by the positive Eoϕ values as indicated by the apparent molar volume data. The caging or packing effect52,53 point toward the positive Eϕo values, indicating the interactions between amino acid and chloramphenicol molecules. An irregular trend is shown by Eoϕ values with an increase in the concentration of chloramphenicol solutions. The structure-making ability of L-leucine/glycyl-Lleucine in all aqueous chloramphenicol solutions is depicted from the positive values of (∂Eoϕ/∂T)p. The second derivative of Voϕ with respect to temperature has negative values for amino acids in water as revealed by data reported in literature,54,55which shows structure-breaking ability of amino acids in water. 3.2. Ultrasonic Properties. 3.2.1. Apparent Molar Isentropic Compression. In aqueous and mixed aqueous solutions of chloramphenicol, the apparent molar isentropic compression for L-leucine and the dipeptide glycyl-L-leucine at different temperatures was determined using equation

Scheme 1. L-Leucine or Glycyl-L-leucine and Chloramphenicol Interactions

solute interactions in these systems are indicated by the negative SV* values. Solute−solute interaction is also influenced by other factors because no regular trend in the S*V values have been found.46 The dominance of solute−solvent interaction over the solute−solute interaction is submitted by the negative values of SV* as compared to positive Voϕ values. Information about the structural volume of the solute in the solvent and the volume change of the solvent in the process of shell formation around the ion is provided by the apparent partial molar volumes, which are known to be sensitive to solute solvation.47,48 By using the eq E2 of the Supporting Information, the transfer volume of amino acid/dipeptide from water to aqueous chloramphenicol solutions at infinite dilution has been calculated, and the values are reported in Table S2 of Supporting Information. For both L-leucine and glycyl-Lleucine, the obtained ΔVoϕ values in Table S2 are all positive and increase with an increase in chloramphenicol concentration. A strong ion−ion interaction of chloramphenicol with L-leucine and glycyl-L-leucine is suggested by the observed positive values of ΔVoϕ. The possibility of various interactions which occur between L-leucine/glycyl-L-leucine and chloramphenicol molecules are mainly: ion−hydrophilic interactions, hydrophilic−hydrophilic interactions, ion−hydrophobic interactions, and hydrophobic−hydrophobic interactions between various constituents of chloramphenicol, amino acid and its dipeptide. As per the cosphere overlap model, a negative contribution is made by ion−hydrophobic interactions and hydrophobic−hydrophobic interactions, whereas ion−hydrophilic and hydrophilic−hydrophilic interactions make a positive contribution to the ΔVoϕ values. Hence, it is deduced that ion− hydrophilic and hydrophilic−hydrophilic interactions are dominating over other interactions in amino acid/dipeptide + water + chloramphenicol mixtures. 3.1.3. Temperature-Dependent Apparent Partial Molar Volume. By using the general polynomial eq E3 given in the Supporting Information, the variation of Voϕ with the temperature can be studied. The values of empirical constants for Lleucine and glycyl-L-leucine in aqueous chloramphenicol solutions are reported in Table S3 of Supporting Information. For both L-leucine and glycyl-L-leucine, the coefficient c has positive values. With the parameters reported in Table S3, the

Kϕ ,s = (Mks/ρ) − {(ks,oρ − ksρo )/mA ρρo }

(2)

where M, mA, ρo, and ρ have the same meaning as given in eq 1. κs,o and κs are the isentropic compressibilities of pure solvent and solution, respectively. By using the following relation, the isentropic compressibility is calculated as

ks = 1/c 2ρ

(3)

where c is the speed of sound, and ρ is the density of the solution. In Table 3, the calculated values of Kϕ,s as well as speed of sound values for molal concentrations (mA) of Lleucine and glycyl-L-leucine in (0.000, 0.0005, 0.001, 0.002, and 0.004) mol·kg−1 chloramphenicol at different temperatures have been outlined. For aqueous solutions of L-leucine and glycyl-L-leucine, the experimental values of speed of sound have been compared with literature values56,57 at different temperatures, as shown in Figures 3 and 4. The experimental speed of sound data is been reported at temperatures T = (228.15, 298.15, 308.15, 318.15) K, whereas in the literature, the speed of sound data has been reported at T = (305.15, 310.15, 315.15) K. The values follow the sequence with temperature 3745



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Table 3. Values of Speeds of Sound, c, and Apparent Molar Isentropic Compression, Kϕ,s of L-Leucine and Glycyl-L-leucine in Aqueous Solutions of Chloramphenicol at Different Temperatures and Experimental Pressure, p = 0.1 MPa c (m·s−1) mAa(mol·kg−1)

T = 288.15 K

T = 298.15 K

Kϕ,s × 106 (m3·mol−1·GPa−1) T = 308.15 K

T = 318.15 K

T = 288.15 K

T = 298.15 K

T = 308.15 K

T = 318.15 K

−40.17 −42.52 −43.63 −44.02 −44.22 −44.36 −44.47 −44.56

−38.91 −41.19 −42.27 −42.65 −42.85 −42.98 −43.09 −43.17

−38.03 −40.29 −41.35 −41.72 −41.92 −42.05 −42.16 −42.24

−40.17 −42.43 −43.65 −44.00 −44.21 −44.34 −44.46 −44.55

−38.90 −41.11 −42.30 −42.64 −42.85 −42.97 −43.08 −43.17

−38.03 −40.20 −41.37 −41.71 −41.92 −42.03 −42.15 −42.23

−40.17 −42.48 −43.59 −43.99 −44.20 −44.33 −44.45 −44.54

−38.90 −41.16 −42.24 −42.63 −42.84 −42.96 −43.07 −43.16

−38.02 −40.25 −41.32 −41.70 −41.91 −42.03 −42.14 −42.22

−40.17 −42.47 −43.60 −43.99 −44.20 −44.33 −44.45 −44.53

−38.99 −41.15 −42.25 −42.63 −42.83 −42.96 −43.07 −43.15

−38.01 −40.24 −41.33 −41.70 −41.90 −42.03 −42.14 −42.22

−40.17 −42.47 −43.58 −43.97 −44.17 −44.30 −44.42 −44.50

−38.98 −41.15 −42.23 −42.61 −42.81 −42.94 −43.05 −43.13

−38.00 −40.25 −41.31 −41.69 −41.88 −42.01 −42.12 −42.20

−40.39 −42.55 −43.67 −44.09 −44.32 −44.47

−39.12 −41.22 −42.32 −42.72 −42.94 −43.09

−38.24 −40.32 −41.39 −41.79 −42.01 −42.16

−1

0.00000b 0.00991 0.02042 0.04026 0.06014 0.08020 0.10017 0.12459 0.15022

1466.73b 1467.97 1469.28 1471.75 1474.23 1476.73 1479.22 1482.26 1485.46

1495.87b 1496.98 1498.16 1500.38 1502.61 1504.86 1507.10 1509.83 1512.70

0.00000b 0.01007 0.01971 0.04149 0.06003 0.08062 0.09922 0.12447 0.14973

1466.86b 1468.12 1469.32 1472.03 1474.34 1476.91 1479.23 1482.38 1485.53

1496.01b 1497.14 1498.22 1500.66 1502.74 1505.04 1507.13 1509.96 1512.79

0.00000b 0.01017 0.02021 0.03985 0.05986 0.08035 0.09955 0.12465 0.14942

1466.98b 1468.26 1469.52 1471.99 1474.50 1477.08 1479.49 1482.65 1485.76

1496.13b 1497.27 1498.39 1500.60 1502.84 1505.13 1507.29 1510.10 1512.87

0.00000b 0.01045 0.02017 0.04036 0.06051 0.08038 0.10071 0.12607 0.15125

1467.12b 1468.44 1469.66 1472.21 1474.75 1477.25 1479.82 1483.01 1486.19

1496.25b 1497.42 1498.51 1500.77 1503.03 1505.26 1507.54 1510.38 1513.20

0.00000b 0.01039 0.02044 0.04027 0.06032 0.08028 0.10003 0.12525 0.15016

1467.48b 1468.80 1470.07 1472.58 1475.12 1477.65 1480.15 1483.35 1486.50

1496.66b 1497.82 1498.95 1501.17 1503.42 1505.66 1507.87 1510.70 1513.49

0.00000b 0.01036 0.02041 0.04005 0.06009 0.08023 0.09965

1466.73b 1468.43 1470.08 1473.30 1476.59 1479.90 1483.09

1495.87b 1497.38 1499.02 1502.01 1505.19 1508.31 1511.32

L-leucine + 0.0000 mol·kg chloramphenicol 1519.50b 1536.12b 1520.49 1537.03 −41.81 1521.55 1538.00 −44.24 1523.54 1539.83 −45.38 1525.53 1541.66 −45.79 1527.54 1543.51 −46.00 1529.55 1545.35 −46.14 1531.99 1547.60 −46.26 1534.56 1549.97 −46.35 −1 L-leucine + 0.0005 mol·kg chloramphenicol b 1519.61 1536.25b 1520.62 1537.18 −41.87 1521.59 1538.07 −44.14 1523.77 1540.07 −45.41 1525.63 1541.78 −45.78 1527.69 1543.68 −45.99 1529.56 1545.40 −46.13 1532.09 1547.72 −46.25 1534.62 1550.05 −46.34 −1 L-leucine + 0.001 mol·kg chloramphenicol b 1519.73 1536.38b 1520.75 1537.32 −41.91 1521.76 1538.24 −44.19 1523.73 1540.05 −45.35 1525.73 1541.90 −45.76 1527.79 1543.79 −45.98 1529.71 1545.56 −46.12 1532.23 1547.87 −46.24 1534.71 1550.15 −46.33 −1 L-leucine + 0.002 mol·kg chloramphenicol 1519.86b 1536.82b 1520.91 1537.78 −42.03 1521.88 1538.70 −44.18 1523.91 1540.53 −45.36 1525.93 1542.38 −45.76 1527.92 1544.22 −45.98 1529.96 1546.04 −46.12 1532.50 1548.36 −46.24 1535.03 1550.66 −46.33 −1 L-leucine + 0.004 mol·kg chloramphenicol b 1520.21 1536.82b 1521.25 1537.84 −41.98 1522.26 1538.66 −44.19 1524.25 1540.62 −45.33 1526.26 1541.96 −45.74 1528.26 1543.85 −45.95 1530.24 1545.57 −46.09 1532.77 1547.86 −46.21 1535.27 1550.03 −46.30 glycyl-L-leucine + 0.0000 mol·kg−1chloramphenicol 1519.50b 1536.12b 1521.05 1537.64 −42.03 1522.56 1539.11 −44.27 1525.50 1542.00 −45.43 1528.51 1544.94 −45.86 1531.52 1547.89 −46.10 1534.43 1550.74 −46.26

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Table 3. continued c (m·s−1) mAa(mol·kg−1)

T = 288.15 K

T = 298.15 K

0.15021 0.20139

1491.39 1499.79

1519.16 1527.10

0.00000b 0.01036 0.02032 0.04039 0.06034 0.08022 0.09911 0.14913 0.19989

1466.86b 1468.56 1470.20 1473.50 1476.78 1480.04 1483.15 1491.37 1499.71

1496.01b 1497.64 1499.20 1502.35 1505.49 1508.61 1511.53 1519.40 1527.35

0.00000b 0.01019 0.02032 0.03986 0.05971 0.07953 0.10031 0.14922 0.19968

1466.98b 1468.65 1470.32 1473.53 1476.79 1480.05 1483.47 1491.51 1499.80

1496.13b 1497.73 1499.32 1502.39 1505.51 1508.62 1511.89 1519.57 1527.50

0.00000b 0.01043 0.02013 0.04061 0.05996 0.08056 0.10002 0.14767 0.19921

1467.12b 1468.84 1470.43 1473.80 1476.99 1480.38 1483.58 1491.42 1499.90

1496.25b 1497.89 1499.41 1502.63 1505.67 1508.90 1511.96 1519.45 1527.54

0.00000b 0.00994 0.02025 0.04021 0.05997 0.08027 0.10009 0.14974 0.19934

1467.48b 1469.12 1470.82 1474.11 1477.37 1480.72 1483.99 1492.17 1500.35

1496.66b 1498.22 1499.84 1502.98 1506.08 1509.27 1512.38 1520.18 1527.97

Kϕ,s × 106 (m3·mol−1·GPa−1) T = 308.15 K

T = 318.15 K

T = 288.15 K

1542.01 1558.16 −46.53 1549.68 1565.67 −46.72 glycyl-L-leucine + 0.0005 mol·kg−1chloramphenicol 1519.61b 1536.25b 1521.16 1537.77 −42.02 1522.66 1539.23 −44.25 1525.66 1542.18 −45.43 1528.65 1545.10 −45.86 1531.63 1548.02 −46.09 1534.46 1550.79 −46.25 1541.96 1558.13 −46.51 1549.57 1565.58 −46.70 glycyl-L-leucine + 0.001 mol·kg−1chloramphenicol 1519.73b 1536.38b 1521.26 1537.88 −44.94 1522.78 1539.36 −45.06 1525.70 1542.23 −45.41 1528.68 1545.14 −45.84 1531.65 1548.05 −46.08 1534.76 1551.10 −46.25 1542.09 1558.28 −46.51 1549.65 1565.68 −46.70 glycyl-L-leucine + 0.002 mol·kg−1chloramphenicol 1519.86b 1536.82b 1521.42 1538.04 −42.04 1522.88 1539.46 −44.21 1525.95 1542.47 −45.42 1528.85 1545.31 −45.83 1531.93 1548.33 −46.08 1534.85 1551.19 −46.23 1541.99 1558.18 −46.49 1549.71 1565.74 −46.68 glycyl-L-leucine + 0.004 mol·kg−1chloramphenicol 1520.21b 1536.82b 1521.70 1538.29 −41.80 1523.24 1539.81 −44.20 1526.24 1542.76 −45.38 1529.20 1545.68 −45.81 1532.24 1548.68 −46.05 1535.21 1551.61 −46.21 1542.65 1558.94 −46.47 1550.08 1566.27 −46.66

T = 298.15 K

T = 308.15 K

T = 318.15 K

−44.73 −44.91

−43.34 −43.52

−42.40 −42.58

−40.38 −42.53 −43.67 −44.08 −44.31 −44.46 −44.72 −44.90

−39.11 −41.21 −42.32 −42.72 −42.94 −43.08 −43.33 −43.51

−38.24 −40.30 −41.40 −41.79 −42.00 −42.15 −42.39 −42.57

−43.69 −44.72 −44.76 −44.81 −44.85 −44.89 −45.00 −45.10

−39.04 −41.20 −42.30 −42.70 −42.92 −43.08 −43.33 −43.50

−38.16 −40.29 −41.37 −41.77 −41.99 −42.14 −42.38 −42.56

−40.40 −42.49 −43.66 −44.06 −44.30 −44.45 −44.69 −44.88

−39.13 −41.17 −42.31 −42.70 −42.93 −43.07 −43.31 −43.49

−38.25 −40.27 −41.39 −41.77 −41.99 −42.13 −42.37 −42.55

−40.17 −42.48 −43.63 −44.04 −44.27 −44.42 −44.68 −44.85

−38.90 −41.16 −42.28 −42.68 −42.90 −43.05 −43.30 −43.47

−38.03 −40.26 −41.36 −41.75 −41.97 −42.12 −42.36 −42.53

a

mA is the molality of amino acids in aqueous chloramphenicol solutions. bValues of densities taken from our earlier paper;64 standard uncertainties u are u (m) = 2 × 10−5 mol·kg−1, u (T) = 0.01 K, u(c) = 0.5 m·s−1, and u (p) = 0.01 MPa.

leucine. In Table S5 of the Supporting Information, the Koϕ,s and SK* values are reported along with standard errors determined using by least-squares fit. It has been found that solute−solvent interactions58are prevailing in the mixtures as solute−solute interactions are negligible at infinite dilution due to small S*K values. The strong attractive interactions between amino acid/dipeptide and water are attributed by more negative values of Koϕ,s at low temperature.59 The less Koϕ,s values at higher temperatures suggest the release of some water molecules due to decrease in electrostriction. No regular o with trend has been found for the variation of Kϕ,s chloramphenicol concentration. Using the eq E8 of Supporting Information, the apparent partial molar isentropic compressions ΔKoϕ,s of amino acid and

(i.e., values increase with an increase in temperature). The values of K ϕ,s are negative at all temperatures and concentrations of chloramphenicol, as observed from the data reported in Table 3. With an increase in temperature, the Kϕ,s values become less negative. The negative Kϕ,s values signify that water molecules in the bulk solution are more compressible than water molecules surrounding the ionic charged groups of amino acid/dipeptide, indicating the strong solute−solvent interactions between ions of amino acid/ dipeptide and drug molecules. 3.2.2. Apparent Partial Molar Isentropic Compression. Equation E7 of Supporting Information can be used to represent the variation of apparent molar isentropic compression Kϕ,s with the molal concentration of L-leucine and glycyl-L3747



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Figure 3. Plots of experimental and literature values (ref 56) of speed of sound for (L-leucine + water) mixtures at different temperatures.

Figure 4. Plots of experimental and literature values (ref 57) of speed of sound for (glycyl-L-leucine + water) mixtures at different temperatures. o values of ΔK ϕ,s has been observed with respect to concentrations of chloramphenicol and temperature. 3.3. Pair and Triplet Interaction Coefficients. Pair and triplet interaction coefficients have been calculated based upon the McMillan−Mayer theory60 of solutions which permits the separation of effects due to interaction between the pairs of solute molecules and those due to its interaction between more than two solute molecules. This theory has further been discussed by Friedmann and Krishnan61so that solute−cosolute

dipeptide from water to aqueous chloramphenicol solutions at infinite dilution were calculated. At all concentrations of chloramphenicol, the values of ΔKoϕ,s reported in Table S6 of the Supporting Information, are all positive for L-leucine and the dipeptide except for L-leucine at low temperature, T = 288.15 K. The dominance of interactions between the zwitterionic center of amino acid/dipeptide and chloramphenicol is predicted by positive values of ΔKoϕ,s indicating the structure making tendency of the ions. An irregular trend in the 3748



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leucine with aqueous chloramphenicol solutions supporting and justifying our thermodynamic data.

interactions can be included in the solvation spheres. So, apparent partial molar volume of transfer and apparent partial molar isentropic compression of transfer can be expressed by eqs E9 and E10 of the Supporting Information. The corresponding parameters VAB, VABB for volume and KAB, KABB for isentropic compression describe pair and triplet interaction coefficients. The values of these parameters obtained by fitting the ΔVoϕ and ΔKoϕ,s values to the eqs E9 and E10 are reported in Table S7 of Supporting Information. For L-leucine and glycyl-L-leucine, the positive values have been observed for the pair interaction coefficients VAB and KAB whereas triplet interaction coefficients VABB and KABB are negative at all temperatures. It is concluded that overlap of hydration spheres62 of solute−cosolute molecules leads to the interactions as suggested by the higher positive values of pair interaction coefficients VAB as compared to negative values of VABB for L-leucine and glycyl-L-leucine. The dominance of pair wise interactions in the ternary mixtures is signified by the positive values of pair interaction coefficient for volumetric and compressibility measurements. 3.4. Absorption Spectral Studies. To analyze the solute− solvent interactions further, the absorption spectra were recorded for different mixtures. In Table 4, we have reported

4. CONCLUSIONS Our results on densities and speeds of sound of L-leucine and glycyl-L-leucine in aqueous chloramphenicol solutions have been reported. From the experimental data, the apparent molar properties and apparent partial molar properties of transfer have been computed. From the interpretation of data, the interactions between L-leucine/glycyl-L-leucine and chloramphenicol molecules are evident. The partial molar properties of transfer suggest strong ion−ion interactions of chloramphenicol molecules with L-leucine/glycyl-L-leucine. The second derivative of temperature (∂2Voϕ/∂T2)p shows the structure-making property of amino acid/dipeptide in aqueous chloramphenicol solution. The dominance of ion−hydrophilic and hydrophilic− hydrophilic interactions in ternary mixtures are revealed by the results obtained from thermodynamic properties. With an increase in the molar mass of solute and the concentration of Lleucine/glycyl-L-leucine and chloramphenicol solution, the extent of interactions increases. The interactions between Lleucine/glycyl-L-leucine and chloramphenicol are also anticipated by the UV absorption data. From the thermodynamic and UV absorption data, it is concluded that solute−solvent interactions increase from L-leucine to glycyl-L-leucine.

Table 4. Absorption Maximum of L-Leucine and Glycyl-Lleucine in Aqueous Solution of Chloramphenicol

■

absorption maximum mAa (mol·kg−1) mBa (mol·kg−1) 0.0005 0.001 0.002 0.004 0.0005 0.001 0.002 0.004

0.02

0.06

L-leucine 1.30 1.82 1.99 2.18 2.14 2.30 2.36 2.44 glycyl-L-leucine 2.48 3.74 3.88 4.07 4.03 4.26 4.39 4.50

ASSOCIATED CONTENT

S Supporting Information *

0.1

0.15

2.07 2.42 2.44 2.64

2.42 2.52 2.64 2.84

4.05 4.25 4.42 4.68

4.36 4.48 4.83 5.15

The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.jced.6b00168. Equations and tables for limiting apparent molar volume, apparent partial molar volume of transfer, temperature dependence of limiting apparent molar volume, limiting apparent molar isentropic compression, apparent partial molar isentropic compression of transfer, pair and triplet interaction coefficients (PDF)

■

AUTHOR INFORMATION

Corresponding Author

*E-mail: [email protected]; [email protected].

a

mB is the molality of aqueous solutions of chloramphenicol and mA is the molality of L-leucine and the dipeptide in aqueous chloramphenicol solutions.

Notes

The authors declare no competing financial interest.

■

ACKNOWLEDGMENTS I.B. acknowledges the Council of Scientific and Industrial Research (CSIR), New Delhi, for providing Junior Research Fellowship (JRF) through sanction order no. (09/1127(0001)/ 2014-EMR-I). The authors also recognize DST, New Delhi, for DST-FIST [CSI-228/2011] Program.

the values of observed absorption maximum. From the Table 4, it is deduced that at a fixed composition of chloramphenicol, the absorption maximum increases with increase in concentration of L-leucine and glycyl-L-leucine. This trend is similar to as observed in case of apparent partial molar volumes. Also, we have recorded the absorption spectra for L-leucine and dipeptide at fixed composition in different aqueous chloramphenicol solutions which shows a regular increase in absorption maximum with increase in chloramphenicol concentration from 0.0005 mol kg−1 to 0.004 mol kg−1 supporting our experimental data. The absorption maximum for glycyl-L-leucine is greater than L-leucine as shown by Table 4. The ions of chloramphenicol coordinate with L-leucine and the dipeptide by breaking the solvent layers of water that causes extended conjugation resonance as indicated by the bathochromic shift observed in case of L-leucine and the dipeptide with chloramphenicol.63 This observation suggest us that interaction increase for mixtures of L-leucine and glycyl-L-

■

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Densities and Speeds of Sound of Antibiotic Drug Chloramphenicol

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