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

ABSTRACT: 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

SUBMITTER: Skvarnavicius G 

PROVIDER: S-EPMC6812127 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature