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Title: Characterization of nanofibers formed by self-assembly of {beta}-peptide oligomers using small angle x-ray scattering

Abstract

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{sub 2}N-{beta}{sup 3}hTyr-{beta}{sup 3}hLys-{beta}{sup 3}hPhe-ACHC-{beta}{sup 3}hPhe-ACHC-{beta}{sup 3}hPhe-{beta}{sup 3}hLys-ACHC-ACHC-{beta}{sup 3}hPhe-{beta}{sup 3}hLys-CONH{sub 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 nanofibersmore » 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.« less

Authors:
;  [1]; ; ; ;  [2]; ;  [3]
  1. Department of Chemical and Biological Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, Wisconsin 53706-1322 (United States)
  2. Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53706-1322 (United States)
  3. Departments of Chemistry and Bioengineering, Rice University, 6100 Main Street, Houston, Texas 77005 (United States)
Publication Date:
OSTI Identifier:
21106225
Resource Type:
Journal Article
Journal Name:
Journal of Chemical Physics
Additional Journal Information:
Journal Volume: 129; Journal Issue: 9; Other Information: DOI: 10.1063/1.2955745; (c) 2008 American Institute of Physics; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0021-9606
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; AMINO ACID SEQUENCE; AQUEOUS SOLUTIONS; FORM FACTORS; NANOSTRUCTURES; PEPTIDES; SMALL ANGLE SCATTERING; STRUCTURE FACTORS; TRANSMISSION ELECTRON MICROSCOPY; X-RAY DIFFRACTION

Citation Formats

Pizzey, Claire L, Abbott, Nicholas L, Pomerantz, William C, Sung, Bong-June, Gellman, Samuel H, Yethiraj, Arun, Yuwono, Virany M, and Hartgerink, Jeffery D. Characterization of nanofibers formed by self-assembly of {beta}-peptide oligomers using small angle x-ray scattering. United States: N. p., 2008. Web. doi:10.1063/1.2955745.
Pizzey, Claire L, Abbott, Nicholas L, Pomerantz, William C, Sung, Bong-June, Gellman, Samuel H, Yethiraj, Arun, Yuwono, Virany M, & Hartgerink, Jeffery D. Characterization of nanofibers formed by self-assembly of {beta}-peptide oligomers using small angle x-ray scattering. United States. https://doi.org/10.1063/1.2955745
Pizzey, Claire L, Abbott, Nicholas L, Pomerantz, William C, Sung, Bong-June, Gellman, Samuel H, Yethiraj, Arun, Yuwono, Virany M, and Hartgerink, Jeffery D. Sun . "Characterization of nanofibers formed by self-assembly of {beta}-peptide oligomers using small angle x-ray scattering". United States. https://doi.org/10.1063/1.2955745.
@article{osti_21106225,
title = {Characterization of nanofibers formed by self-assembly of {beta}-peptide oligomers using small angle x-ray scattering},
author = {Pizzey, Claire L and Abbott, Nicholas L and Pomerantz, William C and Sung, Bong-June and Gellman, Samuel H and Yethiraj, Arun and Yuwono, Virany M and Hartgerink, Jeffery D},
abstractNote = {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{sub 2}N-{beta}{sup 3}hTyr-{beta}{sup 3}hLys-{beta}{sup 3}hPhe-ACHC-{beta}{sup 3}hPhe-ACHC-{beta}{sup 3}hPhe-{beta}{sup 3}hLys-ACHC-ACHC-{beta}{sup 3}hPhe-{beta}{sup 3}hLys-CONH{sub 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.},
doi = {10.1063/1.2955745},
url = {https://www.osti.gov/biblio/21106225}, journal = {Journal of Chemical Physics},
issn = {0021-9606},
number = 9,
volume = 129,
place = {United States},
year = {2008},
month = {9}
}