Molecules of a green fluorescent protein mutant, GFPmut2, have been immobilized in nanocapsules, assemblies of charged polyelectrolyte multilayers, with the aim to study the effect of protein-polyelectrolyte interactions on the protein stability against chemical denaturation. GFPmut2 proteins turn out to be stabilized and protected against the denaturating action of small chemical compounds. The nanocapsule protective effect on GFPmut2 is likely due to protein interactions with the negatively charged polymers, that induce an increase in the local rigidity of the protein nano-environment. This suggestion is supported by Fluorescence Polarization measurements on GFPmut2 proteins bound to the NC layers
Krol, S., Cannone, F., Caccia, M., Sironi, L., Campanini, B., Collini, M., et al. (2008). Structural Stability of Green Fluorescent Proteins Entrapped in Polyelectrolyte Nanocapsules. JOURNAL OF BIOPHOTONICS, 1(4), 310-319 [10.1002/jbio.200810033].
Structural Stability of Green Fluorescent Proteins Entrapped in Polyelectrolyte Nanocapsules
SIRONI, LAURA;COLLINI, MADDALENA;CHIRICO, GIUSEPPE;
2008
Abstract
Molecules of a green fluorescent protein mutant, GFPmut2, have been immobilized in nanocapsules, assemblies of charged polyelectrolyte multilayers, with the aim to study the effect of protein-polyelectrolyte interactions on the protein stability against chemical denaturation. GFPmut2 proteins turn out to be stabilized and protected against the denaturating action of small chemical compounds. The nanocapsule protective effect on GFPmut2 is likely due to protein interactions with the negatively charged polymers, that induce an increase in the local rigidity of the protein nano-environment. This suggestion is supported by Fluorescence Polarization measurements on GFPmut2 proteins bound to the NC layersI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.