Helical oligomers of beta-peptides represent a particularly promising type of building block for directed assembly of organic nanostructures because the helical secondary structure can be designed to be very stable and because control of the beta-amino acid sequence can lead to precise patterning of chemical functional groups over the helix surfaces. In this paper, we report the use of small angle x-ray scattering measurements (SAXS) to characterize nanostructures formed by the directed assembly of beta-peptide A with sequence H(2)N-beta(3)hTyr-beta(3)hLys-beta(3)hPhe-ACHC-beta(3)hPhe-ACHC-beta(3)hPhe-beta(3)hLys-ACHC-ACHC-beta(3)hPhe-beta(3)hLys-CONH(2). Whereas prior cryo-TEM studies have revealed the presence of nanofibers in aqueous solutions of beta-peptide A, SAXS measurements from the nanofibers were not well-fit by a form factor model describing solid nanofibers. An improved fit to the scattering data at high q was obtained by using a form factor model describing a cylinder with a hollow center and radial polydispersity. When combined with a structure factor calculated from the polymer reference interaction site model (PRISM) theory, the scattered intensity of x-rays measured over the entire q range was well described by the model. Analysis of our SAXS data suggests a model in which individual beta-peptides assemble to form long cylindrical nanofibers with a hollow core radius of 15 A (polydispersity of 21%) and a shell thickness of 20 A. This model is supported by negative stain transmission electron microscopy.
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