Peptoid self-assembly and opportunities for creating protein-mimetic biomaterials and biointerfaces

El Yaagoubi, Marwa and Tewari, Kunal M. and Lau, K. H. Aaron; Azevedo, Helena S. and da Silva, Ricardo M.P., eds. (2018) Peptoid self-assembly and opportunities for creating protein-mimetic biomaterials and biointerfaces. In: Self-Assembling Biomaterials. Elsevier, San Diego, pp. 95-112. ISBN 9780081020159

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There is great interest in synthetic polymers that mimic the high degree of functionality observed in peptides and proteins. However, creating a peptidomimetic system that can be easily programmed to present complex structures, biological functions, and morphological features remains a challenge. Specific ordering of diverse monomers in specific sequences to simultaneously encode structural and biochemical functionalities is a hallmark of functional biopolymers. Poly(N-substituted glycines) «peptoids,» prepared using the step-wise solid phase synthesis, constitute a class of novel sequence-specific polymers with a unique combination of bioactivity, synthetic convenience, low immunogenicity, and resistance against proteolysis. Remarkably, these properties arise simply out of a one-atom position shift of the peptide side chain from the alpha-carbon to the amide nitrogen along the peptide backbone. This article reviews the progress in peptoid therapeutics as well as the recent efforts in applying peptoids as alternative materials to peptides and conventional polymers for the self-assembly of nanostructures and for biomedical applications.