Abstract: In vivo, proteins fold into their native states within confining cellular environments. A complete understanding of this folding process, however, is still elusive. Current theories typically do not explicitly consider the interactions between the proteins, the confining surfaces, and the solvent thus treating confinement only as a volume-occupying effect. In this talk I will present a computational model that takes into account these interactions by considering the atomic structure of the confining surface, the solvent water, and a small peptide fragment from the amyloid beta-protein. I will show that by changing the composition of the inner surface of the pore causing the confinement, secondary structure in this peptide can be stabilized or completely destabilized depending on the nature of the inner surface of the pore. I will present our current view that the degree of stability involves the delicate role of the confined solvent on mediating the peptide-surface interactions.