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Antifreeze Glycoproteins Bind Irreversibly to Ice

Cite this: J. Am. Chem. Soc. 2018, 140, 30, 9365–9368
Publication Date (Web):July 20, 2018
https://doi.org/10.1021/jacs.8b04966
Copyright © 2018 American Chemical Society
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Abstract

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Antifreeze proteins (AFPs) and antifreeze glycoproteins (AFGPs) inhibit ice growth via an adsorption-inhibition mechanism that assumes irreversible binding of AF(G)Ps to embryonic ice crystals and the inhibition of further growth. The irreversible binding of antifreeze glycoproteins (AFGPs) to ice has been questioned and remains poorly understood. Here, we used microfluidics and fluorescence microscopy to investigate the nature of the binding of small and large AFGP isoforms. We found that both AFGP isoforms bind irreversibly to ice, as evidenced by microfluidic solution exchange experiments. We measured the adsorption rate of the large AFGP isoform and found it to be 50% faster than that of AFP type III. We also found that the AFGP adsorption rate decreased by 65% in the presence of borate, a well-known inhibitor of AFGP activity. Our results demonstrate that the adsorption rate of AFGPs to ice is crucial for their ice growth inhibition capability.

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The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/jacs.8b04966.

  • Experimental setup, microfluidic solution exchange experiments, adsorption rate measurements, fluorescence intensity calibration, fluorescence intensity of the ice–water interface in the presence of AFGP1–5, effect of borate on the secondary structure of AFGP1–5, and ice growth dynamics in the presence of AFGP7–8 (PDF)

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Cited By

This article is cited by 16 publications.

  1. Pavithra M. Naullage, Valeria Molinero. Slow Propagation of Ice Binding Limits the Ice-Recrystallization Inhibition Efficiency of PVA and Other Flexible Polymers. Journal of the American Chemical Society 2020, 142 (9) , 4356-4366. https://doi.org/10.1021/jacs.9b12943
  2. Tehilla Berger, Konrad Meister, Arthur L. DeVries, Robert Eves, Peter L. Davies, Ran Drori. Synergy between Antifreeze Proteins Is Driven by Complementary Ice-Binding. Journal of the American Chemical Society 2019, 141 (48) , 19144-19150. https://doi.org/10.1021/jacs.9b10905
  3. Poonam Pandey, Asaminew H. Aytenfisu, Alexander D. MacKerell, Jr., Sairam S. Mallajosyula. Drude Polarizable Force Field Parametrization of Carboxylate and N-Acetyl Amine Carbohydrate Derivatives. Journal of Chemical Theory and Computation 2019, 15 (9) , 4982-5000. https://doi.org/10.1021/acs.jctc.9b00327
  4. Toru Ishibe, Thomas Congdon, Christopher Stubbs, Muhammad Hasan, Gabriele C. Sosso, Matthew I. Gibson. Enhancement of Macromolecular Ice Recrystallization Inhibition Activity by Exploiting Depletion Forces. ACS Macro Letters 2019, 8 (8) , 1063-1067. https://doi.org/10.1021/acsmacrolett.9b00386
  5. Christopher Stubbs, Laura E. Wilkins, Alice E. R Fayter, Marc Walker, Matthew I. Gibson. Multivalent Presentation of Ice Recrystallization Inhibiting Polymers on Nanoparticles Retains Activity. Langmuir 2019, 35 (23) , 7347-7353. https://doi.org/10.1021/acs.langmuir.8b01952
  6. Giulia Giubertoni, Konrad Meister, Arthur L. DeVries, Huib J. Bakker. Determination of the Solution Structure of Antifreeze Glycoproteins Using Two-Dimensional Infrared Spectroscopy. The Journal of Physical Chemistry Letters 2019, 10 (3) , 352-357. https://doi.org/10.1021/acs.jpclett.8b03468
  7. Uday Sankar Midya, Sanjoy Bandyopadhyay. Role of Polar and Nonpolar Groups in the Activity of Antifreeze Proteins: A Molecular Dynamics Simulation Study. The Journal of Physical Chemistry B 2018, 122 (40) , 9389-9398. https://doi.org/10.1021/acs.jpcb.8b08506
  8. Aneta Białkowska, Edyta Majewska, Aleksandra Olczak, Aleksandra Twarda-Clapa. Ice Binding Proteins: Diverse Biological Roles and Applications in Different Types of Industry. Biomolecules 2020, 10 (2) , 274. https://doi.org/10.3390/biom10020274
  9. Arthur L. DeVries. Fish Antifreeze Proteins. 2020,,, 85-129. https://doi.org/10.1007/978-3-030-41929-5_5
  10. Maya Bar-Dolev, Koli Basu, Ido Braslavsky, Peter L. Davies. . 2020,,, 69. https://doi.org/10.1007/978-3-030-41948-6_4
  11. Surís-Valls, Voets. Peptidic Antifreeze Materials: Prospects and Challenges. International Journal of Molecular Sciences 2019, 20 (20) , 5149. https://doi.org/10.3390/ijms20205149
  12. Romà Surís-Valls, Ilja K. Voets. The Impact of Salts on the Ice Recrystallization Inhibition Activity of Antifreeze (Glyco)Proteins. Biomolecules 2019, 9 (8) , 347. https://doi.org/10.3390/biom9080347
  13. Yoshinori Furukawa, Ken Nagashima, Shunichi Nakatsubo, Salvador Zepeda, Ken-ichiro Murata, Gen Sazaki. Crystal-plane-dependent effects of antifreeze glycoprotein impurity for ice growth dynamics. Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 2019, 377 (2146) , 20180393. https://doi.org/10.1098/rsta.2018.0393
  14. Cheenou Her, Yin Yeh, Viswanathan V. Krishnan. The Ensemble of Conformations of Antifreeze Glycoproteins (AFGP8): A Study Using Nuclear Magnetic Resonance Spectroscopy. Biomolecules 2019, 9 (6) , 235. https://doi.org/10.3390/biom9060235
  15. Caroline I. Biggs, Christopher Stubbs, Ben Graham, Alice E. R. Fayter, Muhammad Hasan, Matthew I. Gibson. Mimicking the Ice Recrystallization Activity of Biological Antifreezes. When is a New Polymer “Active”?. Macromolecular Bioscience 2019, 7 , 1900082. https://doi.org/10.1002/mabi.201900082
  16. Poonam Pandey, Sairam S. Mallajosyula. Elucidating the role of key structural motifs in antifreeze glycoproteins. Physical Chemistry Chemical Physics 2019, 21 (7) , 3903-3917. https://doi.org/10.1039/C8CP06743K

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