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ARO STIR: Defining Peptide Nanostructures By Engineering Assembly Interfaces

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Final rept. 1 Oct 2012-30 Jun 2013

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This short-term innovative research proposal was focused on the structural characterization of peptide-based, self-assembled nanostructures of specific dimensions that are controlled by the geometry and physicochemical properties of the assembly interface. Our objectives were to i explore solution conditions that allow the production of nanostructures of select structural properties, specifically via the use of gradient hydrophobic interfaces, and ii characterize the conformation, fibril formation, and network properties of these peptide-based materials via a suite of circular dichroic spectroscopy CD, oscillatory rheology, microscopy AFM, SEM, TEM, and scattering SANS methods. We have successfully achieved the aims of this STIR project, and have clearly demonstrated that i beta-hairpin structures can be formed by peptides with gradient hydrophobic faces comprising non-natural amino acids, ii these peptides are competent for fibril formation, and iii fibril formation and branching as indicated by resulting network mechanical properties can be modulated by modifications of the gradient of the hydrophobic interface. Loose packing of the designed fibrils is indicated, on the basis of initial SANS analysis, suggesting opportunities to modify the fibril interface with a range of chemically and electronically diverse hydrophobic amino acids, which will provide new opportunities to make smart materials for in-situ sensing and device fabrication.

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  • Biochemistry

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