In conclusion, our results show the profound effect of the protein corona not only on the SNPs-membrane interaction strength but also on the mechanisms of their interplay. For SNPs-18 we do not have any evidence of diminished membrane affinity of the BSA-coated SNPs with respect to the bare SNPs-18 but we observe a distinct change in the interaction mechanism. On the other hand, the BSA corona on SNPs-30@BSA, while still causing membrane adhesion, suppresses the fusogenic activity of these SNPs and the GUVs do not show clear membrane perturbations or wrapping expected for strong adhesion. The binding affinity of proteins to nanomaterials depends principally on the type of protein, the surface properties of the NPs and their size . The different membrane responses produced by these two types of SNPs@BSA might therefore be related to differences in the protein corona formed on the surface of NPs of different sizes but it also suggests that even after the corona is formed, the inherent NP properties still influence the membrane interaction. This may be rationalised by the fact that the corona is physisorbed on the NP surface and therefore the BSA might be partially displaced by the SNP-lipid interaction on the membrane surface. Further studies with coronas made of different proteins and other relevant biomacromolecules are needed to understand and predict the fate of NPs within biological systems. This will eventually enable fabrication of safe-by-design nanomaterials that retain their desired functions in complex biological media without harmful side effects.