Trp-cage is an artificial miniprotein that is small, stable, and fast folding due to concerted hydrophobic shielding of a Trp residue by polyproline helices. Simulations have extensively characterized TT-cage; however, the interactions of Trp-cage with organic surfaces (e.g., membranes) and their effect on protein conformation are largely unknown. To better understand these interactions we utilized a combination of replica-exchange molecular dynamics (REMD) and metadynamics (MetaD), to investigate Ttp-cage folding on self-assembled monolayers (SAMs). We found that, with REMD and MetaD, Trp-cage strongly binds to neutral CH, surfaces (-25kT) and moderately adsorbs to anionic COOH interfaces (-7.6kT), with hydrophobic interactions driving CH, adhesion and electrostatic attractions driving COOH adhesion. Similar to solid-state surfaces, SAMs facilitate a number of intermediate Tip-cage conformations between folded and unfolded states. Regarding Tip-cage's aromatic groups in neutral CH, systems, Tyr becomes oriented parallel to the surface in order to maximize hydrophobic interactions while Tip remains caged perpendicular to the surface; however, Tip can reorient itself parallel to the interface as the miniprotein more closely binds to the surface. In contrast, Tyr and Tip are both repelled from COOH surfaces, though the Tip-cage still adheres to the anionic interface via Lys and its N-terminated Asn residue.