Thermochemistry of the Dissolution of Dipeptides Containing DL-α-Alanine in Aqueous Solutions of Sodium Dodecyl Sulfate at 298.15 K

被引:4
|
作者
Smirnov, V. I. [1 ]
Badelin, V. G. [1 ]
机构
[1] Russian Acad Sci, Krestov Inst Solut Chem, Ivanovo 153045, Russia
基金
俄罗斯基础研究基金会;
关键词
peptides; enthalpy of dissolution; sodium dodecyl sulfate; ternary mixtures; AMINO-ACIDS; THERMODYNAMIC CHARACTERISTICS; ELLIPSOIDAL MICELLES; WATER; ENTHALPIES; SURFACTANT; SOLVENTS; AMIDES; GLYCYLGLYCYLGLYCINE; GLYCYLGLYCINE;
D O I
10.1134/S003602441805028X
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Enthalpies of the dissolution of DL-alpha-alanylglycine (AlaGly), DL-alpha-alanyl-DL-alpha-alanine (AlaAla), DL-alpha-alanyl-DL-alpha-valine (AlaVal), and DL-alpha-alanyl-DL-norleucine (AlaNln) in an aqueous solution of sodium dodecyl sulfate (SDS) at SDS concentration of m = 0-0.07 mol kg(-1) and temperature T = 298.15 K are measured via calorimetry. The standard values of the enthalpy of dissolution (Delta H-sol(m)) and the transfer of dipeptides (Delta H-tr(m) ) from water to aqueous SDS solutions are calculated using the experimental data. The dependences of Delta H-sol(m) and Delta H-tr(m) the SDS concentration at a constant concentration of dipeptide are established. Thermochemical characteristics of the transfer of AlaGly, AlaAla, AlaVal, and AlaNln in the investigated range of SDS concentrations are compared. The results are interpreted by considering ion-ion, ion-polar, and hydrophobic-hydrophobic interactions between SDS and dipeptide molecules.
引用
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页码:900 / 904
页数:5
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