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Article

The Inhibition of Icing and Frosting on Glass Surfaces by the Coating of Polyethylene Glycol and Polypeptide Mimicking Antifreeze Protein

1
Division of Mechanophysics, Graduate School of Science and Technology, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
2
Faculty of Molecular Chemistry and Engineering, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
3
School of Environment, Science and Engineering, Southern Cross University, Military Road, Lismore 2480, NSW, Australia
4
Faculty of Mechanical Engineering, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
*
Author to whom correspondence should be addressed.
Biomolecules 2020, 10(2), 259; https://doi.org/10.3390/biom10020259
Submission received: 29 December 2019 / Revised: 19 January 2020 / Accepted: 6 February 2020 / Published: 9 February 2020
(This article belongs to the Special Issue Effects of Biomolecules on Ice Nucleation)

Abstract

The development of anti-icing, anti-frosting transparent plates is important for many reasons, such as poor visibility through the ice-covered windshields of vehicles. We have fabricated new glass surfaces coated with polypeptides which mimic a part of winter flounder antifreeze protein. We adopted glutaraldehyde and polyethylene glycol as linkers between these polypeptides and silane coupling agents applied to the glass surfaces. We have measured the contact angle, the temperature of water droplets on the cooling surfaces, and the frost weight. In addition, we have conducted surface roughness observation and surface elemental analysis. It was found that peaks in the height profile, obtained with the atomic force microscope for the polypeptide-coated surface with polyethylene glycol, were much higher than those for the surface without the polypeptide. This shows the adhesion of many polypeptide aggregates to the polyethylene glycol locally. The average supercooling temperature of the droplet for the polypeptide-coated surface with the polyethylene glycol was lower than for the polypeptide-coated surface with glutaraldehyde and the polyethylene-glycol-coated surface without the polypeptide. In addition, the average weight of frost cover on the specimen was lowest for the polypeptide-coated surface with the polyethylene glycol. These results argue for the effects of combined polyethylene glycol and polypeptide aggregates on the locations of ice nuclei and condensation droplets. Thus, this polypeptide-coating with the polyethylene glycol is a potential contender to improve the anti-icing and anti-frosting of glasses.
Keywords: polypeptide; aggregate; antifreeze protein; polyethylene glycol; glass surface; anti-icing; anti-frosting; supercooling temperature; surface roughness polypeptide; aggregate; antifreeze protein; polyethylene glycol; glass surface; anti-icing; anti-frosting; supercooling temperature; surface roughness

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MDPI and ACS Style

Kasahara, K.; Waku, T.; Wilson, P.W.; Tonooka, T.; Hagiwara, Y. The Inhibition of Icing and Frosting on Glass Surfaces by the Coating of Polyethylene Glycol and Polypeptide Mimicking Antifreeze Protein. Biomolecules 2020, 10, 259. https://doi.org/10.3390/biom10020259

AMA Style

Kasahara K, Waku T, Wilson PW, Tonooka T, Hagiwara Y. The Inhibition of Icing and Frosting on Glass Surfaces by the Coating of Polyethylene Glycol and Polypeptide Mimicking Antifreeze Protein. Biomolecules. 2020; 10(2):259. https://doi.org/10.3390/biom10020259

Chicago/Turabian Style

Kasahara, Kazuya, Tomonori Waku, Peter W. Wilson, Taishi Tonooka, and Yoshimichi Hagiwara. 2020. "The Inhibition of Icing and Frosting on Glass Surfaces by the Coating of Polyethylene Glycol and Polypeptide Mimicking Antifreeze Protein" Biomolecules 10, no. 2: 259. https://doi.org/10.3390/biom10020259

APA Style

Kasahara, K., Waku, T., Wilson, P. W., Tonooka, T., & Hagiwara, Y. (2020). The Inhibition of Icing and Frosting on Glass Surfaces by the Coating of Polyethylene Glycol and Polypeptide Mimicking Antifreeze Protein. Biomolecules, 10(2), 259. https://doi.org/10.3390/biom10020259

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