jp6b08213_si_001.pdf (5.84 MB)
Residue-Specific Interactions of an Intrinsically Disordered Protein with Silica Nanoparticles and Their Quantitative Prediction
journal contribution
posted on 2016-09-21, 00:00 authored by Mouzhe Xie, Alexandar
L. Hansen, Jiaqi Yuan, Rafael BrüschweilerElucidation
of the driving forces that govern interactions between
nanoparticles and intrinsically disordered proteins (IDP) is important
for the understanding of the effect of nanoparticles in living systems
and for the design of new nanoparticle-based assays to monitor health
and combat disease. The quantitative interaction profile of the intrinsically
disordered transactivation domain of p53 and its mutants with anionic
silica nanoparticles is reported at atomic resolution using nuclear
magnetic spin relaxation experiments. These profiles are analyzed
with a novel interaction model that is based on a quantitative nanoparticle
affinity scale separately derived for the 20 natural amino acids.
The results demonstrate how the interplay of attractive and repulsive
Coulomb interactions with hydrophobic effects is responsible for the
sequence-dependent binding of a disordered protein to nanoparticles.
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novel interaction modelIDPp 53Silica Nanoparticlesnanoparticle-based assayscombat diseaseproteinsequence-dependent bindingResidue-Specific Interactionsrelaxation experimentsIntrinsically Disordered Proteininteraction profileCoulomb interactionstransactivation domainnanoparticle affinity scaleQuantitative Prediction Elucidationsilica nanoparticles
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