AbstractAll efforts to turn the ultimate goal in proteinde novodesign into reality–the construction of new macromolecules with predetermined three‐dimensional structure and well‐defined functionality–failed because the mechanism of folding has still to be unravelled. In the present review, various attempts to apply synthetic tools for inducing native‐like structural features in peptides in order to bypass the folding problem are described. Besides well‐established methods for the nucleation and stabilization of secondary structures, e.g. α‐helices, β‐sheets and β‐turns, topological templates as ‘built‐in’ folding devices have more recently become the key elements for the induction of protein‐like folding units (template‐assembled synthetic proteins, TASP). Progress in the synthetic strategy and structural characterization of this new type of macromolecules opens the way for the desig