Interactions of Polyproline II Helix Peptides with Iron(III) Oxide

Loney, Charles N.; Perez Bakovic, Sergio I.; Xu, Cheyan; Graybill, Ashley; Greenlee, Lauren F.; Renner, Julie N.

doi:10.1002/slct.201901817

Title: Interactions of Polyproline II Helix Peptides with Iron(III) Oxide

Abstract

Interactions of a peptide with polyproline II helical secondary structure with maghemite (iron(III) oxide, Fe₂O₃) surfaces were characterized using a variety of surface techniques. A quartz crystal microbalance with dissipation was used to measure the hydrated mass and thickness (92 ± 29 ng/cm² and 0.89 ± 0.27 nm, respectively) of a layer which formed after a sensor coated with Fe₂O₃ was exposed to the peptide in aqueous solution. The analysis revealed that the peptide formed a stable thin layer on the sensor. X-ray photoelectron spectroscopy and Fourier-transform infrared spectroscopy of the monolayer were employed to study the relationship between the metal and the peptide. Finally, Fe₂O₃ nanoparticles were incubated with the peptide, and analysis of the settling and particle size revealed that the presence of the peptide reduced the occurrence of large aggregates in solution.

Authors:

Loney, Charles N. ^[1]; Perez Bakovic, Sergio I. ^[2]; Xu, Cheyan ^[1]; Graybill, Ashley ^[1]; Greenlee, Lauren F. ^[2]; Renner, Julie N. ^[1]

Case Western Reserve Univ., Cleveland, OH (United States)
Univ. of Arkansas, Fayetteville, AR (United States)

Publication Date:: Tue Jun 11 00:00:00 EDT 2019

Research Org.:: Univ. of Arkansas, Fayetteville, AR (United States)

Sponsoring Org.:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

OSTI Identifier:: 1542899

Grant/Contract Number:: SC0016529

Resource Type:: Accepted Manuscript

Journal Name:: Chemistry Select

Additional Journal Information:: Journal Volume: 4; Journal Issue: 22; Journal ID: ISSN 2365-6549

Publisher:: Wiley

Country of Publication:: United States

Language:: English

Subject:: 36 MATERIALS SCIENCE

Citation Formats


                    Loney, Charles N., Perez Bakovic, Sergio I., Xu, Cheyan, Graybill, Ashley, Greenlee, Lauren F., and Renner, Julie N. Interactions of Polyproline II Helix Peptides with Iron(III) Oxide.  United States: N. p., 2019. 
Web.  doi:10.1002/slct.201901817.

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                    Loney, Charles N., Perez Bakovic, Sergio I., Xu, Cheyan, Graybill, Ashley, Greenlee, Lauren F., & Renner, Julie N. Interactions of Polyproline II Helix Peptides with Iron(III) Oxide.  United States.  https://doi.org/10.1002/slct.201901817

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                    Loney, Charles N., Perez Bakovic, Sergio I., Xu, Cheyan, Graybill, Ashley, Greenlee, Lauren F., and Renner, Julie N. Tue .  
"Interactions of Polyproline II Helix Peptides with Iron(III) Oxide".  United States.  https://doi.org/10.1002/slct.201901817.  https://www.osti.gov/servlets/purl/1542899.

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@article{osti_1542899,

  title        = {Interactions of Polyproline II Helix Peptides with Iron(III) Oxide},

  author       = {Loney, Charles N. and Perez Bakovic, Sergio I. and Xu, Cheyan and Graybill, Ashley and Greenlee, Lauren F. and Renner, Julie N.},

  abstractNote = {Interactions of a peptide with polyproline II helical secondary structure with maghemite (iron(III) oxide, Fe2O3) surfaces were characterized using a variety of surface techniques. A quartz crystal microbalance with dissipation was used to measure the hydrated mass and thickness (92 ± 29 ng/cm2 and 0.89 ± 0.27 nm, respectively) of a layer which formed after a sensor coated with Fe2O3 was exposed to the peptide in aqueous solution. The analysis revealed that the peptide formed a stable thin layer on the sensor. X-ray photoelectron spectroscopy and Fourier-transform infrared spectroscopy of the monolayer were employed to study the relationship between the metal and the peptide. Finally, Fe2O3 nanoparticles were incubated with the peptide, and analysis of the settling and particle size revealed that the presence of the peptide reduced the occurrence of large aggregates in solution.},

  doi          = {10.1002/slct.201901817},

  journal      = {Chemistry Select},

  number       = 22,

  volume       = 4,

  place        = {United States},

  year         = {Tue Jun 11 00:00:00 EDT 2019},

  month        = {Tue Jun 11 00:00:00 EDT 2019}

}

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Title: Interactions of Polyproline II Helix Peptides with Iron(III) Oxide

Abstract

Citation Formats

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QCM-D and Reflectometry Instrument: Applications to Supported Lipid Structures and Their Biomolecular Interactions journal, January 2009

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Beware of connective tissue proteins: Assignment and implications of collagen absorptions in infrared spectra of human tissues journal, January 1995

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Left-handed Polyproline II Helices Commonly Occur in Globular Proteins
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QCM-D and Reflectometry Instrument: Applications to Supported Lipid Structures and Their Biomolecular Interactions
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