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

Journal Article · · Chemistry Select
 [1];  [2];  [3];  [3];  [2];  [3]
  1. Case Western Reserve Univ., Cleveland, OH (United States); University of Arkansas
  2. Univ. of Arkansas, Fayetteville, AR (United States)
  3. Case Western Reserve Univ., Cleveland, OH (United States)

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.

Research Organization:
Univ. of Arkansas, Fayetteville, AR (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Grant/Contract Number:
SC0016529
OSTI ID:
1542899
Journal Information:
Chemistry Select, Journal Name: Chemistry Select Journal Issue: 22 Vol. 4; ISSN 2365-6549
Publisher:
WileyCopyright Statement
Country of Publication:
United States
Language:
English

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