A hallmark feature of proteins is their ability to encode molecular interactions in the monomer sequence to control the folding of the polymer chains into higher order structures and intermolecular assemblies. The development of iterative chemical synthesis has enabled access to compositionally diverse oligomers or polymers having defined monomer sequences. In this presentation, our recent efforts in the synthesis of linearly amphiphilic peptoid oligomers where the number and position of the ionizable groups are precisely defined along the oligomer chains and investigation of their self-assembly in solution will be discussed. The position and pattern of charges along the chains have a pronounced effect on the micellar structures in water. Such effect can be quantitatively described by scaling relationships.

Investigating the role of sequence-defined charges on the solution self-assemblies of discrete amphiphilic peptoid oligomers

2019 Fall National Meeting

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