“…Especially, the hydrophobic interaction between the hydrophobic domain and the hydrophobic surface of insulin exposed by part denaturation is very important, and is the main driving force for the denaturation of the insulin-FITC native structure. 19,24,[29][30][31][32] Possibly due to part denaturation, it was observed that the hydrophilic insulin-FITC molecules immediately became precipitate, when adding peptide RATEA16 into its aqueous solution (see Supporting Information). At the same time, the extent to b-sheet secondary structure of peptide increased, indicating that the existence of insulin-FITC molecules redounded to the b-sheet formation of peptide RATEA16.…”