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- W3067622178 abstract "In this work, we examine the electronic and morphological consequences of constitutional isomerism in tri- and tetrablock biohybrid self-assembling molecules that display three regimes of “hydrophobic” composition. A solubilizing hydrophilic peptide head group is attached covalently to a π-conjugated oligothiophene unit that undergoes π–π stacking interactions and introduces a unique quadrupolar character, a hydrophobic peptide segment that encourages hydrogen bonding, and in some cases, a terminal n-alkyl tail that further triggers hydrophobic collapse. We examine constitutional isomerism by swapping the presentation of these disparate hydrophobic blocks in these complex π-conjugated peptides. We found that constitutional isomerism in molecules containing two peptide segments and the π-conjugated oligomer greatly impacts solubility, nanostructure lateral bundling, and the mode of molecular packing that ultimately dictates electronic communication among the π-conjugated units. Furthermore, we found that this effect is not diluted by the addition of an n-alkyl tail that also provides access to a range of nanoarchitectures from spheres to elongated micellar structures, rods, and ribbons." @default.
- W3067622178 created "2020-08-24" @default.
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- W3067622178 date "2020-08-18" @default.
- W3067622178 modified "2023-10-18" @default.
- W3067622178 title "A Tale of Three Hydrophobicities: Impact of Constitutional Isomerism on Nanostructure Evolution and Electronic Communication in π-Conjugated Peptides" @default.
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- W3067622178 doi "https://doi.org/10.1021/acs.macromol.0c01492" @default.
- W3067622178 hasPublicationYear "2020" @default.
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