Publication:
Applications of type I antifreeze proteins: Studies with model membranes & cryoprotectant properties

dc.contributor.author Inglis, Steven en_US
dc.contributor.author Turner, J en_US
dc.contributor.author Harding, Margaret en_US
dc.date.accessioned 2021-11-25T13:30:39Z
dc.date.available 2021-11-25T13:30:39Z
dc.date.issued 2006 en_US
dc.description.abstract Antifreeze proteins (AFPs) and antifreeze glycoproteins (AFGPs), found in the body fluids of many species of polar fish allow them to survive in waters colder than the equilibrium freezing point of their blood and other internal fluids. Despite their structural diversity, all AF(G)Ps kinetically depress the temperature at which ice grows in a noncolligative manner and hence exhibit thermal hysteresis. AF(G)Ps also share the ability to interact with and protect mammalian cells and tissues from hypothermic damage (e.g., improved storage of human blood platelets at low temperatures), and are able to stabilize or disrupt membrane composition during low temperature and freezing stress (e.g., cryoprotectant properties in stabilization of sperm and oocytes). This review will summarize studies of AFPs with phospholipids and plant lipids, proposed mechanisms for inhibition of leakage from membranes, and cryoprotectant studies with biological samples. The major focus will be on the alpha-helical type I antifreeze proteins, and synthetic mutants, that have been most widely studied. For completeness, data on glycoproteins will also be presented. While a number of models to explain stabilization and destabilization of different lipid systems have been proposed, it is currently not possible to predict whether a particular AFP will stabilize or destabilize a given lipid system. Furthermore the relationship between the antifreeze property of thermal hysteresis and membrane stabilization is unknown. This lack of detailed knowledge about how AFPs function in the presence of different types of materials has hampered progress toward the development of antifreezes for cold storage of cells, tissues, and organs. en_US
dc.identifier.issn 1389-2037 en_US
dc.identifier.uri http://hdl.handle.net/1959.4/39840
dc.language English
dc.language.iso EN en_US
dc.rights CC BY-NC-ND 3.0 en_US
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/3.0/au/ en_US
dc.source Legacy MARC en_US
dc.subject.other antifreeze en_US
dc.subject.other helical protein en_US
dc.subject.other glycoprotein en_US
dc.subject.other membranes en_US
dc.subject.other cryoprotectant en_US
dc.title Applications of type I antifreeze proteins: Studies with model membranes & cryoprotectant properties en_US
dc.type Journal Article en
dcterms.accessRights metadata only access
dspace.entity.type Publication en_US
unsw.accessRights.uri http://purl.org/coar/access_right/c_14cb
unsw.description.notePublic Original inactive link: http://www.benthamdirect.org/pages/content.php?CPPS/2006/00000007/00000006/0006K.SGM en_US
unsw.relation.faculty Science
unsw.relation.ispartofissue 6 en_US
unsw.relation.ispartofjournal Current Protein & Peptide Science en_US
unsw.relation.ispartofpagefrompageto 509-522 en_US
unsw.relation.ispartofvolume 7 en_US
unsw.relation.originalPublicationAffiliation Inglis, Steven en_US
unsw.relation.originalPublicationAffiliation Turner, J en_US
unsw.relation.originalPublicationAffiliation Harding, Margaret, Chemistry, Faculty of Science, UNSW en_US
unsw.relation.school School of Chemistry *
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