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

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

Deadline for manuscript submissions: 30 April 2018

Special Issue Editors

Guest Editor
Prof. Dr. Hak Jun Kim

Pukyong National University, Department of Chemistry,Busan, Korea
Website | E-Mail
Interests: ice-binding proteins; antifreeze protein; cold-active enzyme; membrane protein; cold-adaptation
Guest Editor
Prof. Dr. Jun Hyuck Lee

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
Website | E-Mail
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

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Marine Drugs is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


  • 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

Published Papers (1 paper)

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Open AccessArticle Identification and Characterization of an Isoform Antifreeze Protein from the Antarctic Marine Diatom, Chaetoceros neogracile and Suggestion of the Core Region
Mar. Drugs 2017, 15(10), 318; doi:10.3390/md15100318 (registering DOI)
Received: 13 September 2017 / Revised: 13 October 2017 / Accepted: 16 October 2017 / Published: 18 October 2017
PDF Full-text (4588 KB) | HTML Full-text | XML Full-text | Supplementary Files
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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