Quantitative Binding Behavior of Intrinsically Disordered Proteins to Nanoparticle Surfaces at Individual Residue Level

Chemistry : a European Journal
Mouzhe XieRafael Brüschweiler

Abstract

The quantitative and predictive understanding how intrinsically disordered proteins (IDPs) interact with engineered nanoparticles has potentially important implications for new therapeutics as well as nanotoxicology. Based on a recently developed solution 15 N NMR relaxation approach, the interactions between four representative IDPs with silica nanoparticles are reported at atomic detail. Each IDP possesses distinct binding modes, which can be quantitatively explained by the local amino-acid residue composition using a "free residue interaction model". The model was parameterized using the binding affinities of free proteinogenic amino acids along with long-range effects, derived by site-specific mutagenesis, that exponentially scale with distance along the primary sequence. The model, which is accessible through a web server, can be applied to predict the residue-specific binding affinities of a large number of IDPs.

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Citations

Aug 30, 2020·International Journal of Molecular Sciences·Joao V de SouzaAgnieszka K Bronowska
Dec 3, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Mariapina D'OnofrioMichael Assfalg
Sep 11, 2020·Angewandte Chemie·Stacey WardenfeltRafael Brüschweiler
Nov 1, 2019·Israel Journal of Chemistry·Y Randika PereraNicholas C Fitzkee
May 20, 2020·Journal of the American Chemical Society·Da-Wei LiRafael Brüschweiler
Dec 1, 2020·The Journal of Physical Chemistry Letters·Mouzhe Xie, Rafael Brüschweiler
Dec 29, 2020·Langmuir : the ACS Journal of Surfaces and Colloids·Hui Xu, Leah Beck Casabianca

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