Thermodynamics of Interactions Between Charged Surfactants and Ionic Poly(amino acids) by Isothermal Titration Calorimetry

Thermodynamics of Interactions Between Charged Surfactants and Ionic Poly(amino acids) by Isothermal Titration Calorimetry
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通过等温滴定量热法研究带电表面活性剂与离子聚氨基酸之间相互作用的热力学

DOI:
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发表时间:
2019
期刊:
影响因子:
4.1
通讯作者:
V. Petrauskas
V. Petrauskas
中科院分区:
化学3区
文献类型:
--
作者:
Gediminas Skvarnavičius;Danielius Dvareckas;D. Matulis;V. Petrauskas

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Interactions between charges play a role in protein stability and contribute to the energetics of binding between various charged ligands. Ionic surfactants are charged molecules, whose interactions with proteins are still rather poorly understood despite their wide applications. Here, we show by isothermal titration calorimetry that cationic alkylammonium surfactants bind to negatively charged polyaspartate and polyglutamate homopolymers stoichiometrically, i.e., one surfactant molecule per charged amino acid. Similarly, negatively charged alkyl sulfates (e.g., sodium dodecyl sulfate) and alkane sulfonates bind stoichiometrically to positively charged polylysine, polyornithine, and polyarginine homopolymers. In these reactions, the interacting counterparts form ion pairs and the resulting electrostatically neutral complex coprecipitates from solution. The enthalpies and heat capacities are determined for various pairs of ionic surfactants and charged amino acid homopolymers. These results show the energetic contributions of ionic headgroups and the CH2 group to surfactant interactions with proteins.
DOI: 10.1073/pnas.88.7.2854
发表时间: 1991
影响因子: 11.1
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