Statistical analysis regarding the chemico-physical properties of NPs was performed using the Student's t-Test, where * p < 0.05 and ** p < 0.01, included in the software GraphPad Prism 6 (GraphPad Holdings, San Diego, CA, USA). All results are the mean with standard deviation (SD) measuring at least 3 different samples: n > 3.
Protein identification was achieved by searching the protein databases Swiss-Prot (2018_05, Homo Sapiens 557,491 entries) for peptides, and c-RAP for contaminants (ftp://ftp.thegpm.org/fasta/cRAP , 116 entries), using the MASCOT protein identification software (Version 2.4, Matrix Science, London, UK). Once identified, proteins were semi-quantified by normalizing their presence to the total amount of proteins and expressed using the “exponentially modified Protein Abundance Index” (emPAI) (Arike and Peil, 2014 (link)).
Eventually, results were statistically evaluated with the MSStat tool (Choi et al., 2014 (link)) and graphed as volcano plots with the binary logarithm of the fold change between two samples in the x-axis and the –log2 of the adjusted p on the y-axis. Proteins present in the PC with a log fold change < −2 or > 2 and an adjusted p < 0.05 were considered statistically differently between samples.
Protein identification was achieved by searching the protein databases Swiss-Prot (2018_05, Homo Sapiens 557,491 entries) for peptides, and c-RAP for contaminants (
Eventually, results were statistically evaluated with the MSStat tool (Choi et al., 2014 (link)) and graphed as volcano plots with the binary logarithm of the fold change between two samples in the x-axis and the –log2 of the adjusted p on the y-axis. Proteins present in the PC with a log fold change < −2 or > 2 and an adjusted p < 0.05 were considered statistically differently between samples.