We present a full thermodynamic study of the binding of lysozyme and human serum albumin (HSA) to dendritic polyglycerolsulfate (dPGS) in aqueous solution. We discuss and model the free energy of binding as the function of the salt concentration c<sub>s </sub>and the temperature <i>T</i>. Both systems exhibit a strong enthalpy-entropy compensation throughout the entire range of temperature, similar to the one observed for the interaction of DNA with various proteins. We demonstrate that the free energy of binding can be split into a part solely due to counterion release and a residual part in full agreement with MD-simulations. We also studied the    adsorption    of    Human    Serum    Albumin    (HSA)    onto    spherical    polyelectrolyte    brushes  (SPB)  by  isothermal  titration  calorimetry  (ITC). Again ITC  measurements  done  at  different  temperatures  and  ionic  strengths  were performed that lead  to  a  full  set  of  thermodynamic  data including  the  enthalpies  and  entropies  of  binding. The analysis demonstrated that this system exhibits also a strong enthalpy-entropy cancellation. A  comparison  with  the  analysis  of  other  sets  of  data  related  to  the  binding  of  HSA  to  polyelectrolytes  suggests that the  EEC  is  a  general  phenomenon that accompanies the binding of proteins to highly hydrated structures as e.g. dPGS or DNA.

Interaction of proteins with polyelectrolytes: Free polyelectrolytes vs. polyelectrolyte brushes

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.