Antifreeze glycoproteins: relationship between molecular weight, thermal hysteresis and the inhibition of leakage from liposomes during thermotropic phase transition

Wu, Yaling; Banoub, Joseph; Goddard, Stephen; Kao, Ming H.; Fletcher, George P.

doi:10.1016/s1096-4959(00)00323-7

Cited by 61 publications

(46 citation statements)

References 22 publications

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“…The reason that the large isoform has higher activity than the small one is presumably because the ice-binding side of the former is four times larger. This assumption falls into line with the observation that larger isoforms of AFPs are generally more active than the smaller ones (Schrag et al, 1982;Wu et al, 2001).…”

Section: Controlling the Freezing Process With Antifreeze Proteinssupporting

confidence: 80%

Controlling the Freezing Process with Antifreeze Proteins

Ramløv

Johnsen

2014

Emerging Technologies for Food Processing

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Section: Controlling the Freezing Process With Antifreeze Proteinssupporting

confidence: 80%

Controlling the Freezing Process with Antifreeze Proteins

Ramløv

Johnsen

2014

Emerging Technologies for Food Processing

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“…Wu, Banoub, Goddard, Kao, and Fletcher (2001) found that the AFPs prevented leakage from diethy pyrocarbonate (DEPC) liposomes as they were cooled through their phase transition temperature. Yao et al (2014) investigated the relationship among membrane damage, leakage of intracellular proteins of Escherichia coli treated by pressurized CO 2 .…”

Section: Effect Of App On the Intracellular Proteins And Nucleic Acidmentioning

confidence: 99%

Hypothermia protection effect of antifreeze peptides from pigskin collagen on freeze-dried Streptococcus thermophiles and its possible action mechanism

Wang

Chen

et al. 2015

LWT - Food Science and Technology

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“…While early studies suggested that AFPs could block or alter the flow of ions into cells [62,73,74], more recent studies have demonstrated that AFPs and AFGPs are able to protect cell membranes as they pass through their phase transition temperatures [79][80][81][82][83][84] ( Table 5). A number of studies have been performed with a range of model membranes in order to fully understand the origin of these interactions, and as a result some insight into the interaction(s) between TTTT and AFGPs and different membranes has emerged.…”

Section: Interactions With Model Membrane Systemsmentioning

confidence: 99%

Applications of Type I Antifreeze Proteins: Studies with Model Membranes & Cryoprotectant Properties

Inglis¹,

Turner²,

Harding³

2006

CPPS

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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 non-colligative 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.

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Antifreeze glycoproteins: relationship between molecular weight, thermal hysteresis and the inhibition of leakage from liposomes during thermotropic phase transition

Cited by 61 publications

References 22 publications

Controlling the Freezing Process with Antifreeze Proteins

Controlling the Freezing Process with Antifreeze Proteins

Hypothermia protection effect of antifreeze peptides from pigskin collagen on freeze-dried Streptococcus thermophiles and its possible action mechanism

Applications of Type I Antifreeze Proteins: Studies with Model Membranes & Cryoprotectant Properties

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