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Issue 14, 2018
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Designing phenylalanine-based hybrid biological materials: controlling morphology via molecular composition

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Abstract

Harnessing the self-assembly of peptide sequences has demonstrated great promise in the domain of creating high precision shape-tunable biomaterials. The unique properties of peptides allow for a building block approach to material design. In this study, self-assembly of mixed systems encompassing two peptide sequences with identical hydrophobic regions and distinct polar segments is investigated. The two peptide sequences are diphenylalanine and phenylalanine-asparagine-phenylalanine. The study examines the impact of molecular composition (namely, the total peptide concentration and the relative tripeptide concentration) on the morphology of the self-assembled hybrid biological material. We report a rich polymorphism in the assemblies of these peptides and explain the relationship between the peptide sequence, concentration and the morphology of the supramolecular assembly.

Graphical abstract: Designing phenylalanine-based hybrid biological materials: controlling morphology via molecular composition

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Publication details

The article was received on 16 Jan 2018, accepted on 10 Mar 2018 and first published on 14 Mar 2018


Article type: Paper
DOI: 10.1039/C8OB00130H
Citation: Org. Biomol. Chem., 2018,16, 2499-2507
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    Designing phenylalanine-based hybrid biological materials: controlling morphology via molecular composition

    S. Mushnoori, K. Schmidt, V. Nanda and M. Dutt, Org. Biomol. Chem., 2018, 16, 2499
    DOI: 10.1039/C8OB00130H

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