Aim: nanoparticle-cell interactions can promote cell toxicity and stimulate particular behavioral patterns, but cell responses to protein nanomaterials have been poorly studied. - Results: by repositioning oligomerization domains in a simple, modular self-assembling protein platform, we have generated closely related but distinguishable homomeric nanoparticles. Composed by building blocks with modular domains arranged in different order, they share amino acid composition. These materials, once exposed to cultured cells, are differentially internalized in absence of toxicity and trigger distinctive cell adaptive responses, monitored by the emission of tubular filopodia and enhanced drug sensitivity. - Conclusion: the capability to rapidly modulate such cell responses by conventional protein engineering reveals protein nanoparticles as tuneable, versatile and potent cell stressors for cell-targeted conditioning.
Anglès
Molecular therapy; Nanoparticles; Recombinant proteins; Self-assembling; Stressor
Agència de Gestió d'Ajuts Universitaris i de Recerca 2014/SGR-132
Agència de Gestió d'Ajuts Universitaris i de Recerca 2017/FIB100063
Instituto de Salud Carlos III PI15/00272
Nanomedicine ; Vol. 13, issue 3 (Feb. 2018), p. 255-268
open access
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