Marine Ice-binding Proteins and Their Mimetics: Structure, Function, and Application

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (30 April 2018) | Viewed by 10187

Special Issue Editors


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Guest Editor
Department of Chemistry, Pukyong National University, Busan 48513, Republic of Korea
Interests: cold-active enzymes; psychrophilic proteins; ice-binding proteins; antifreeze proteins; cold-adaptation
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Guest Editor
1. Unit of Polar Genomics, Korea Polar Research Institute (KOPRI), Incheon, Republic of Korea
2. Department of Polar Sciences, Korea University of Science and Technology, Incheon, Republic of Korea
Interests: ice-binding proteins; antifreeze protein; structure and function of psychrophilic protein

Special Issue Information

Dear Colleagues,

Ice-binding proteins are a group of proteins that have affinity for ice. Antifreeze proteins, the most commonly-known terminology for this kind of protein, are a misnomer since they are actually a subset of ice-binding protein and some, not all, ice-binding proteins function as a biological antifreeze in physiological concentrations. In this Special Issue, we would like to use “ice-binding proteins” to include any proteins that have affinity for ice, such as antifreeze proteins, ice nucleation proteins, ice-recrystallization inhibition proteins, and ice-interacting proteins.

Since the fish antifreeze proteins were first identified in the late 1960s, the number of ice-binding proteins identified from marine organisms has been continuously increasing. Currently, ice-binding proteins are found in bacteria, fungi, microalgae, and crustaceans inhabiting cold environments. Marine ice-binding proteins seem to possess characteristic ice-binding sites, despite their diversity in primary and tertiary structures. The ice-binding affinity is well manifested in their properties: Thermal hysteresis and ice-recrystallization inhibition. In addition, some ice-binding proteins appear to interact with biological membranes. These properties are of biotechnological interest for cryopreservation of valuable biological resources, such as stem cells.

This Special Issue, "Marine Ice-Binding Proteins and Their Mimetics: Structure, Function, and Applications", of Marine Drugs will cover, but is not limited to, reviews and recent results regarding the isolation and characterization of new marine ice-binding genes and proteins, structure determination, and application of ice-binding proteins, mimetic peptides and/or peptoids in various fields, such as cryopreservation and hypothermic storage.

Prof. Dr. Hak Jun Kim
Prof. Dr. Jun Hyuck Lee
Guest Editors

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Keywords

  • Marine ice-binding proteins

  • Marine antifreeze proteins

  • Marine antifreeze glycoproteins

  • Marine antifreeze peptides

  • Horizontal gene transfer

  • Psychrophiles

  • Peptidomimetics

  • Ice-binding affinity

  • Ice recrystallization inhibition

  • Thermal hysteresis

  • Membrane interaction

  • X-ray structure

  • NMR

  • Molecular dynamics simulations

  • Cryopreservation

  • Vitrification

  • Heterologous expression

  • Gene organization

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Published Papers (2 papers)

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Research

1723 KiB  
Short Note
Effect of Marine-Derived Ice-Binding Proteins on the Cryopreservation of Marine Microalgae
by Hak Jun Kim, Bon-Won Koo, Doa Kim, Ye Seul Seo and Yoon Kwon Nam
Mar. Drugs 2017, 15(12), 372; https://doi.org/10.3390/md15120372 - 1 Dec 2017
Cited by 7 | Viewed by 4074
Abstract
Ice-binding protein (IBPs) protect cells from cryo-injury during cryopreservation by inhibiting ice recrystallization (IR), which is a main cause of cell death. In the present study, we employed two IBPs, one, designated LeIBP from Arctic yeast, and the other, designated FfIBP from Antarctic [...] Read more.
Ice-binding protein (IBPs) protect cells from cryo-injury during cryopreservation by inhibiting ice recrystallization (IR), which is a main cause of cell death. In the present study, we employed two IBPs, one, designated LeIBP from Arctic yeast, and the other, designated FfIBP from Antarctic sea ice bacterium, in the cryopreservation of three economically valuable marine microalgae, Isochrysis galbana, Pavlova viridis, and Chlamydomonas coccoides. Both of the IBPs showed IR inhibition in f/2 medium containing 10% DMSO, indicating that they retain their function in freezing media. Microalgal cells were frozen in 10% DMSO with or without IBP. Post-thaw viability exhibited that the supplementation of IBPs increased the viability of all cryopreserved cells. LeIBP was effective in P. viridis and C. coccoides, while FfIBP was in I. galbana. The cryopreservative effect was more drastic with P. viridis when 0.05 mg/mL LeIBP was used. These results clearly demonstrate that IBPs could improve the viability of cryopreserved microalgal cells. Full article
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4588 KiB  
Article
Identification and Characterization of an Isoform Antifreeze Protein from the Antarctic Marine Diatom, Chaetoceros neogracile and Suggestion of the Core Region
by Minjae Kim, Yunho Gwak, Woongsic Jung and EonSeon Jin
Mar. Drugs 2017, 15(10), 318; https://doi.org/10.3390/md15100318 - 18 Oct 2017
Cited by 10 | Viewed by 5334
Abstract
Antifreeze proteins (AFPs) protecting the cells against freezing are produced in response to extremely low temperatures in diverse psychrophilic organisms, and they are encoded by multiple gene families. The AFP of Antarctic marine diatom Chaetoceros neogracile is reported in our previous research, but [...] Read more.
Antifreeze proteins (AFPs) protecting the cells against freezing are produced in response to extremely low temperatures in diverse psychrophilic organisms, and they are encoded by multiple gene families. The AFP of Antarctic marine diatom Chaetoceros neogracile is reported in our previous research, but like other microalgae, was considered to probably have additional genes coding AFPs. In this paper, we reported the cloning and characterization of additional AFP gene from C. neogracile (Cn-isoAFP). Cn-isoAFP protein is 74.6% identical to the previously reported Cn-AFP. The promoter sequence of Cn-isoAFP contains environmental stress responsive elements for cold, thermal, and high light conditions. Cn-isoAFP transcription levels increased dramatically when cells were exposed to freezing (−20 °C), thermal (10 °C), or high light (600 μmol photon m−2 s−1) stresses. The thermal hysteresis (TH) activity of recombinant Cn-isoAFP was 0.8 °C at a protein concentration of 5 mg/mL. Results from homology modeling and TH activity analysis of site-directed mutant proteins elucidated AFP mechanism to be a result of flatness of B-face maintained via hydrophobic interactions. Full article
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