Fiber-like materials from oxazolidin-2-ones containing pseudopeptides

Aggregation and disaggregation are central phenomena in nature.1 In this context, formation of fibers through self-assembly is of particular interest, as protein fibers are involved in intra- and extracellular functions. Moreover, several diseases such as Alzheimer’s or prion diseases are induced by amyloid peptides or proteins that tend to accumulate and aggregate in extracellular space. This process is thermodynamically favorable, since -sheet layers are the most stable proteinacious superstructure in nature. Oligopeptides may be designed and prepared with the aim of interfering with the pathological aggregation of proteins.2 Here, we report the synthesis of oligomers of hybrid peptides with the general formula Boc-(L-Phe-D-Oxd)n-OBn with n = 1-5, that were investigated both in solution and in the solid state, employing several experimental techniques.