The shape of these peptide amphiphiles can be roughly. approximated by three cylindrical regions where Region 11 (in black) is made up of the hydrophobic alkane tail: "Hydrophobic interactions" drive the formation of self-assembled structures to minimize the contact of hydrophobic regions with the aqueous solution. Based on experimental studies, the average AG increase. to form an interface between longer hydrophobic alkanes and water is about +35 ml/m² at 298K. 1 For a single peptide amphiphile, assume that Region 1 is approximately 2.0 nm long and forms a cylinder with radius, r=0.2 nm. Use this to estimate the Gibbs energy change (AGhydrophobic) in kJ/mol when a peptide amphiphile is removed from a nanofiber into aqueous solution. 1

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