Probing the protein corona around charged macromolecules: interpretation of isothermal titration calorimetry by binding models and computer simulations

Abstract: Isothermal titration calorimetry (ITC) is a widely used tool to experimentally probe the heat signal of the formation of the protein corona around macromolecules or nanoparticles. If an appropriate binding model is applied to the ITC data, the heat of binding and the binding stoichiometry as well as the binding affinity per protein can be quantified and interpreted. However, the binding of the protein to the macromolecule is governed by complex microscopic interactions. In particular, due to the steric and electrostatic protein–protein interactions within the corona as well as cooperative, charge renormalization effects of the total complex, the application of standard (e.g., Langmuir) binding models is questionable and the development of more appropriate binding models is very challenging. Here, we discuss recent developments in the interpretation of the Langmuir model applied to ITC data of protein corona formation, exemplified for the well-defined case of lysozyme coating highly charged dendritic polyglycerol sulfate (dPGS), and demonstrate that meaningful data can be extracted from the fits if properly analyzed. As we show, this is particular useful for the interpretation of ITC data by molecular computer simulations where binding affinities can be calculated but it is often not clear how to consistently compare them with the ITC data. Moreover, we discuss the connection of Langmuir models to continuum binding models (where no discrete binding sites have to be assumed) and their possible extensions toward the inclusion of leading order cooperative electrostatic effects

Object Details

• Location: Deutsche Nationalbibliothek Frankfurt am Main
• Extent: Online-Ressource
• Language: Englisch
• Notes: Colloid and polymer science. - 298, 7 (2020) , 747-759, ISSN: 1435-1536

Contributors, Places and Time

• Event: Veröffentlichung
• (where): Freiburg
• (who): Universität
• (when): 2021
• Creator: Xu, Xiao ; Dzubiella, Joachim

Further information

• DOI: 10.1007/s00396-020-04648-x
• URN: urn:nbn:de:bsz:25-freidok-2197543
• Rights: Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Last update: 14.08.2025, 10:49 AM CEST