Author ORCID Identifier

Cheyan Xu

Julie N. Renner

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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.


iron(III) oxide, nanoparticles, peptides, polyproline II helix, quartz crystal microbalance with dissipation

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U.S. Department of Energy, Office of Science, Basic Energy Sciences, Catalysis Science Program;


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This is the peer reviewed version of the following article: C. N. Loney, S. I. Perez Bakovic, C. Xu, A. Graybill, L. F. Greenlee, J. N. Renner, Interactions of Polyproline II Helix Peptides with Iron(III) Oxide, ChemistrySelect 2019, 4, 6784, which has been published in final form at




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