Angiogenin is a
protein crucial in angiogenesis, and it is overexpressed in many
cancers and downregulated in
neurodegenerative diseases, respectively. The
protein interaction with actin, through the loop encompassing the 60-68 residues, is an essential step in the cellular cytoskeleton reorganization. This, in turn, influences the cell proliferation and migration processes. In this work, hybrid nanoassemblies of
gold nanoparticles with
angiogenin fragments containing the 60-68 sequence were prepared and characterized in their interaction with both model membranes of supported
lipid bilayers (SLBs) and cellular membranes of
cancer (
neuroblastoma) and normal (fibroblasts) cell lines. The comparison between physisorption and chemisorption mechanisms was performed by the parallel investigation of the 60-68 sequence and the
peptide analogous containing an extra
cysteine residue. Moreover, steric hindrance and charge effects were considered with a third analogous
peptide sequence, conjugated with a fluorescent
carboxyfluorescein (Fam) moiety. The hybrid nanobiointerface was characterized by means of ultraviolet-visible, atomic force microscopy and circular dichroism, to scrutinize plasmonic changes, nanoparticles coverage and conformational features, respectively. Lateral diffusion measurements on SLBs "perturbed" by the interaction with the
gold nanoparticles-
peptides point to a stronger membrane interaction in comparison with the uncoated nanoparticles. Cell viability and proliferation assays indicate a slight nanotoxicity in
neuroblastoma cells and a proliferative activity in fibroblasts. The actin staining confirms different levels of interaction between the hybrid assemblies and the cell membranes.