In recent years, many protein-protein interactions (PPIs) have been defined as new druggable targets, where small molecules typically show an inferior capacity in interference with such PPIs. Larger structures able to interfere with the considerably increased surface area typically associated with PPIs are therefore needed. In this context the power of peptide and protein based structures has now been recognized not in the least because of the impressive selectivities that have been observed. However, peptide-based compounds typically behave badly in terms of metabolic and conformational stability. In current project we propose an approach to equip peptides with stable conformational behavior and increased metabolic stability through attachment of the peptide sequence of interest onto a steroid scaffold. More specifically, a cholic acid based template is proposed and different ligation strategies are defined to obtain a series of stabilised helices and conformationally stabilised loops that feature the desired capacities for application in different disease areas. In previous research at OBCR, the cholic acid moiety has been shown to endow the appended peptides with increased serum stability as well as increased bioavailability. Adittionally the cholic acid motif has been observed to allow for better membrane association and cell-uptake thus equipping the peptides with enhanced pharmacokinetic properties upon cyclisation.