Characterization of nanofibers formed by self-assembly of Β-peptide oligomers using small angle x-ray scattering

Claire L. Pizzey; William C. Pomerantz; Bong June Sung; Virany M. Yuwono; Samuel H. Gellman; Jeffery D. Hartgerink; Arun Yethiraj; Nicholas L. Abbott

doi:10.1063/1.2955745

Characterization of nanofibers formed by self-assembly of Β-peptide oligomers using small angle x-ray scattering

Claire L. Pizzey, William C. Pomerantz, Bong June Sung, Virany M. Yuwono, Samuel H. Gellman, Jeffery D. Hartgerink, Arun Yethiraj, Nicholas L. Abbott

Chemistry (Twin Cities)

Research output: Contribution to journal › Article › peer-review

38 Scopus citations

Abstract

Helical oligomers of Β -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 Β -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 Β -peptide A with sequence H2 N- Β3 hTyr- Β3 hLys- Β3 hPhe-ACHC- Β3 hPhe-ACHC- Β3 hPhe- Β3 hLys-ACHC-ACHC- Β3 hPhe- Β3 hLys-CON H2. Whereas prior cryo-TEM studies have revealed the presence of nanofibers in aqueous solutions of Β -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 Β -peptides assemble to form long cylindrical nanofibers with a hollow core radius of 15 Å (polydispersity of 21%) and a shell thickness of 20 Å. This model is supported by negative stain transmission electron microscopy.

Original language	English (US)
Article number	095103
Journal	Journal of Chemical Physics
Volume	129
Issue number	9
DOIs	https://doi.org/10.1063/1.2955745
State	Published - 2008

Bibliographical note

Funding Information:
This research was supported by UW–Madison Nanoscale Science and Engineering Center (NSF Grant No. DMR-0425880). We thank Bruker AXS (Fitchburg, WI) and Dr. Kurt Erlacher for providing access to the x-ray facilities used in this work. V.M.Y. was supported by the Robert A. Welch Foundation research Grant No. C1557.

Access

10.1063/1.2955745

OpenUrl availability

Full text

Cite this

@article{cb73f41ce4224695b8f076567d69b78a,

title = "Characterization of nanofibers formed by self-assembly of Β-peptide oligomers using small angle x-ray scattering",

abstract = "Helical oligomers of Β -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 Β -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 Β -peptide A with sequence H2 N- Β3 hTyr- Β3 hLys- Β3 hPhe-ACHC- Β3 hPhe-ACHC- Β3 hPhe- Β3 hLys-ACHC-ACHC- Β3 hPhe- Β3 hLys-CON H2. Whereas prior cryo-TEM studies have revealed the presence of nanofibers in aqueous solutions of Β -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 Β -peptides assemble to form long cylindrical nanofibers with a hollow core radius of 15 {\AA} (polydispersity of 21%) and a shell thickness of 20 {\AA}. This model is supported by negative stain transmission electron microscopy.",

author = "Pizzey, {Claire L.} and Pomerantz, {William C.} and Sung, {Bong June} and Yuwono, {Virany M.} and Gellman, {Samuel H.} and Hartgerink, {Jeffery D.} and Arun Yethiraj and Abbott, {Nicholas L.}",

note = "Funding Information: This research was supported by UW–Madison Nanoscale Science and Engineering Center (NSF Grant No. DMR-0425880). We thank Bruker AXS (Fitchburg, WI) and Dr. Kurt Erlacher for providing access to the x-ray facilities used in this work. V.M.Y. was supported by the Robert A. Welch Foundation research Grant No. C1557.",

year = "2008",

doi = "10.1063/1.2955745",

language = "English (US)",

volume = "129",

journal = "Journal of Chemical Physics",

issn = "0021-9606",

publisher = "American Institute of Physics Publising LLC",

number = "9",

}

TY - JOUR

T1 - Characterization of nanofibers formed by self-assembly of Β-peptide oligomers using small angle x-ray scattering

AU - Pizzey, Claire L.

AU - Pomerantz, William C.

AU - Sung, Bong June

AU - Yuwono, Virany M.

AU - Gellman, Samuel H.

AU - Hartgerink, Jeffery D.

AU - Yethiraj, Arun

AU - Abbott, Nicholas L.

N1 - Funding Information: This research was supported by UW–Madison Nanoscale Science and Engineering Center (NSF Grant No. DMR-0425880). We thank Bruker AXS (Fitchburg, WI) and Dr. Kurt Erlacher for providing access to the x-ray facilities used in this work. V.M.Y. was supported by the Robert A. Welch Foundation research Grant No. C1557.

PY - 2008

Y1 - 2008

N2 - Helical oligomers of Β -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 Β -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 Β -peptide A with sequence H2 N- Β3 hTyr- Β3 hLys- Β3 hPhe-ACHC- Β3 hPhe-ACHC- Β3 hPhe- Β3 hLys-ACHC-ACHC- Β3 hPhe- Β3 hLys-CON H2. Whereas prior cryo-TEM studies have revealed the presence of nanofibers in aqueous solutions of Β -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 Β -peptides assemble to form long cylindrical nanofibers with a hollow core radius of 15 Å (polydispersity of 21%) and a shell thickness of 20 Å. This model is supported by negative stain transmission electron microscopy.

AB - Helical oligomers of Β -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 Β -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 Β -peptide A with sequence H2 N- Β3 hTyr- Β3 hLys- Β3 hPhe-ACHC- Β3 hPhe-ACHC- Β3 hPhe- Β3 hLys-ACHC-ACHC- Β3 hPhe- Β3 hLys-CON H2. Whereas prior cryo-TEM studies have revealed the presence of nanofibers in aqueous solutions of Β -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 Β -peptides assemble to form long cylindrical nanofibers with a hollow core radius of 15 Å (polydispersity of 21%) and a shell thickness of 20 Å. This model is supported by negative stain transmission electron microscopy.

UR - http://www.scopus.com/inward/record.url?scp=51349111182&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=51349111182&partnerID=8YFLogxK

U2 - 10.1063/1.2955745

DO - 10.1063/1.2955745

M3 - Article

C2 - 19044891

AN - SCOPUS:51349111182

SN - 0021-9606

VL - 129

JO - Journal of Chemical Physics

JF - Journal of Chemical Physics

IS - 9

M1 - 095103

ER -

Characterization of nanofibers formed by self-assembly of Β-peptide oligomers using small angle x-ray scattering

Abstract

Bibliographical note

Access

OpenUrl availability

Other files and links

Fingerprint

Cite this