“…However, a weak positive charge from the globular BSA protein can provide a sufficient drift for adsorption at an interface (Su et al, 1998a;Jachimska et al, 2016). Multiple articles have previously reported the adsorption of BSA and similar proteins near the isoelectric point to be driven by hydrophobic interactions which outweigh the electrostatic interactions (Uyen et al, 1990;Tilton et al, 1991;Figueira and Jones, 2008;Norde, 2008;Jeyachandran et al, 2009;Rabe et al, 2011;Huang et al, 2017;Xu et al, 2018;Attwood et al, 2019). The contact angle measurements (Figure 5) show the bare gold interface is less hydrophobic, and albumin binds with gold via hydrophobic interactions (Norde and Giacomelli, 2000;Figueira and Jones, 2008).…”