The ability to make predictable three-dimensional materials is an area of explicit interest, especially in the realm of peptides. Peptoids offer an advantage over peptides for areas such as drug delivery due to their enhanced resistance to metabolic degradation. However, peptoids have a significant disadvantage compared to peptides because the structural benefits from hydrogen bonding and rigidity in the backbone are missing due to side chain substitution at the nitrogen atom instead of the α-carbon. It is known that specific placement of aromatic and/or bulky sidechains can induce secondary structure in peptoids and form α-helical polymers. Peptoids are also known to form β-sheets like peptides. These structural elements are formed through non-covalent interactions such as π-stacking and Van der Waals interactions. This work demonstrates our ability to exploit these interactions to create secondary structure as well as encourage these structures to interact through space to make larger three-dimensional, highly structured foldamers in a defined manner. The synthesis of hydrophilic peptoids and structural data on these polymers demonstrates that a three-dimensional structure based on non-covalent interactions between peptoid units generates predictable foldamer geometries.

Designing foldamers: Synthesis of hydrophilic peptoids that fold in a predictable manner

253rd National Meeting (2017)

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