H. Kumar, K.

Kaur / Journal of Molecular Liquids 173 (2012) 130–136 133

Table 2
Limiting apparent molar volumes, Vϕ0 and experimental slopes, SV⁎ of alanine, valine and leucine in aqueous solutions of ampicillin at different temperatures.

m/(mol kg−1) Vϕ0 × 106/(m3 mol−1) SV*× 106/(m3 l1/2 mol−3/2)

T = 305.15 K T = 310.15 K T = 315.15 K T = 305.15 K T = 310.15 K T = 315.15 K

Alanine
0.000 60.27(±0.05) 60.53(±0.02) 60.83(± 0.02) 241.72(±6.62) 252.67(±2.49) 258.11(±2.30)
0.0006 60.42(±0.02) 61.02(±0.03) 62.02(± 0.03) 263.54(±2.15) 277.31(±0.37) 260.82(±2.97)
0.001 60.90(±0.07) 62.26(±0.06) 63.78(± 0.03) 133.72(±8.19) 173.01(±7.23) 182.89(±3.51)
0.002 62.13(±0.08) 63.12(±0.07) 64.34(± 0.05) 199.51(±9.54) 240.09(±8.31) 239.35(±6.85)
0.004 63.48(±0.14) 65.33(±0.09) 67.20(± 0.04) 224.79(±18.19) 227.38(±13.38) 188.31(±5.24)

Valine
0.000 90.95(±0.05) 91.27(±0.05) 91.58(± 0.05) 228.12(±2.63) 240.48(±5.48) 240.98(±5.43)
0.0006 91.51(±0.04) 94.41(±0.06) 97.05(± 0.08) 312.58(±4.98) 318.11(±6.45) 305.65(±8.92)
0.001 91.97(±0.06) 95.66(±0.11) 98.59(± 0.03) 274.91(±7.71) 216.34(±12.89) 221.33(±3.27)
0.002 92.87(±0.05) 96.28(±0.07) 99.32(± 0.08) 508.33(±7.05) 477.03(±10.29) 520.69(±10.72)
0.004 94.11(±0.10) 97.06(±0.06) 101.47(0.11) 176.65(12.70) 217.21(7.33) 213.84(13.04)

Leucine
0.000 106.97(0.11) 107.34(0.07) 107.65(0.06) 162.26(12.33) 187.52(8.14) 209.45(7.49)
0.0006 107.19(0.03) 108.15(0.05) 109.13 (0.09) 302.73(3.55) 320.92(4.99) 318.80(9.87)
0.001 108.33(0.08) 114.42(0.08) 117.88(0.12) 405.78(9.69) 254.19(9.16) 319.08(13.96)
0.002 109.53(0.04) 116.25(0.12) 121.51(0.22) 248.91(5.60) 180.23(14.45) 234.95(26.85)
0.004 110.04(0.12) 119.15(0.19) 125.44(0.14) 172.73(14.10) 222.42(22.91) 190.81(16.62)

interactions. The partial molar volume of aqueous solutions of drugs
can be divided into four main contributions [18,19].
0
V ϕ ¼ V ðINÞ þ V ðCOULÞ þ V ðSTRÞ þ V ðHBÞ
where V(IN) is the intrinsic property of solute before interactions
takes place, V(COUL) is electrostriction of solvent caused by coulom-
bic interactions among solvent and the drug (negative effect), V(STR)
is the overall structural contribution to volume that includes any
cavity formation (negative effect) and any increase in ice likeness of
water (positive effect) due to changes in the structure of water and
V(HB) is the contribution which arises due to hydrogen bonding
between solute and drug solution. The actual contribution [20] of
V(COUL) and V(STR) may be considered due to (a) Influence of
electrical field on the water molecules around the ion through ion–
dipole interactions and (b) orientation of water molecules to have
suitable geometry, so as to have three dimensional hydrogen bonded
network. So the structuring of water will depend on the ion, its size
and shape, and number of group. Partial molal volumes are known
to be sensitive to solute salvation, it provides information about
structural volume of solute in solvent and volume change of solvent
in the process of shell formation around the ion [21]. In present
case, Vϕ0 increases by increasing molar mass and size i.e. leucine hav-
ing higher molar mass have highest value of Vϕ0 and glycine having
lower molar mass have lowest value of Vϕ0. Further, for all the amino
cosphere overlap model [22]. From Table 3 it is clear that the
magnitude of transfer is higher and it becomes higher and higher as
we move from alanine to leucine because of the effect of adding
ð3Þ chain except at higher concentration of AMP and also for all amino
acids transfer volume increases as we go from lower concentration
to higher concentration which is obvious because of more ion-ion or
hydrophilic-hydrophilic interactions. The explanation for this behav-
ior lies in fact that the interaction increases because of interaction of
the hydrogen bond between protonated amino group of AMP and
ionized carboxylic group of amino acid and also with the ionized car-
boxylic group and the protonated amino group of amino acids as both
are amphoteric.
The apparent molar adiabatic compressibility for all amino acids in
aqueous and mixed aqueous solutions at different temperatures was
determined by using following equation
 
K ϕ;s ¼ MβS =ρ þ 1000=mρρ0 βS ρ0 −βS;0 ρ ð5Þ
where m is the molality (mol kg−1) of the solution, M is the molar mass
of the solute(kg mol−1) and ρ0 and ρ are the densities (kg m −3) of the
Table 3
Partial molar volume of transfer, ΔVϕ0 of glycine, alanine and leucine in aqueous solu-
tions of AMP at different temperatures.

acids ranging from alanine to leucine, Vϕ0 increases with increase in m/(mol kg−1) ΔVϕ0 × 106/(m3 mol−1)
drug concentration i.e. from 0.0005 mol kg −1 to 0.004 mol kg −1 of
T = 305.15 K T = 310.15 K T = 315.15 K
AMP. Transfer volume of amino acids from water to aqueous AMP
Alanine
solutions at infinite dilution were calculated by using the equation
0.0006 0.15 0.49 1.19
0 0 0
0.001 0.63 1.73 2.95
ΔV ϕ ¼ Vϕ ðin aq: AMP solutionÞ−V ϕ ðin waterÞ ð4Þ 0.002 1.86 2.59 3.51
0.004 3.21 4.8 6.37
The calculated values of ΔVϕ0 as reported in Table 3 are all positive
Valine
which suggests strong ion–ion interactions of drug ampicillin with 0.0006 0.56 3.14 5.47
amino acids. The structural moiety of drug bears polar groups like 0.001 1.02 4.39 7.01
amino group and carboxylic acid group and also the solute that is 0.002 1.92 5.01 7.74
0.004 3.16 5.79 9.89
amino acids contain polar groups in their structure therefore interac-
tions between these two promotes the structure i.e. structure maker Leucine
ability of solute in the solution. In the present investigation the 0.0006 0.22 0.81 1.48
observed positive values of transfer volume suggest that structure 0.001 1.36 7.08 10.23
promoter nature of these solutes is due to their solvophobic salvation 0.002 2.56 8.91 13.86
0.004 3.07 11.81 17.79
as well as the structural interaction for two co-spheres according to