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- W2346202150 abstract "The exquisite self-assembly of proteins and peptides in nature into highly ordered functional materials has inspired innovative approaches to the design and synthesis of biomimetic materials. While sequence-defined polymers hold great promise to mimic proteins and peptides for functions, controlled assembly of them on surfaces still remains underdeveloped. Here, we report the assembly of 12-mer peptoids containing alternating acidic and aromatic monomers into networks of hexagonally patterned nanoribbons on mica surfaces. Ca(2+)-carboxylate coordination creates peptoid-peptoid and peptoid-mica interactions that control self-assembly. In situ atomic force microscopy (AFM) shows that peptoids first assemble into discrete nanoparticles; these particles then transform into hexagonally patterned nanoribbons on mica surfaces. AFM-based dynamic force spectroscopy studies show that peptoid-mica interactions are much stronger than peptoid-peptoid interactions, illuminating the driving forces for mica-directed peptoid assembly. We further demonstrate the display of functional domains at the N-terminus of assembling peptoids to produce extended networks with similar hierarchical structures. This research demonstrates that surface-directed peptoid assembly can be used as a robust platform to develop biomimetic coating materials for applications." @default.
- W2346202150 created "2016-06-24" @default.
- W2346202150 creator A5024089820 @default.
- W2346202150 creator A5032588260 @default.
- W2346202150 creator A5051150181 @default.
- W2346202150 date "2016-05-09" @default.
- W2346202150 modified "2023-09-29" @default.
- W2346202150 title "Surface-Directed Assembly of Sequence-Defined Synthetic Polymers into Networks of Hexagonally Patterned Nanoribbons with Controlled Functionalities" @default.
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- W2346202150 doi "https://doi.org/10.1021/acsnano.6b01333" @default.
- W2346202150 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27136277" @default.
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