Structure and function of antifreeze proteins

Davies, Peter L.; Baardsnes, Jason; Kuiper, Michael J.; Walker, Virginia K.

doi:10.1098/rstb.2002.1081

Cited by 279 publications

(281 citation statements)

References 35 publications

(52 reference statements)

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“…Details on these topics can be found in other review papers and books. 1, [17][18][19][20]40 Structure of AFPs AFPs are classified into several types according to the features of their three-dimensional structure (Figure 1). Type-I AFPs have a simple a-helical structure.…”

Section: Fundamentals Of Afpsmentioning

confidence: 99%

Antifreeze proteins: computer simulation studies on the mechanism of ice growth inhibition

Nada

Furukawa

2012

Polym J

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Antifreeze proteins (AFPs), which are present in the bodily fluids of organisms inhabiting cold environments, function as inhibitors of ice growth by binding to certain planes of ice crystals. However, the exact mechanism of ice growth inhibition is still poorly understood as it is exceedingly difficult to experimentally analyze the molecular-scale growth kinetics of ice crystals at the planes to which the proteins bind. This review paper focuses on computer simulation studies on the mechanism of ice growth inhibition by AFPs. Recent molecular dynamics simulations of a growing ice-water interface to which protein is bound have indicated that, when the protein is stably bound to the interface, the growth rate of ice surrounding the protein decreases drastically, owing to depression of the ice melting point through the Gibbs-Thomson effect. The observed decrease in growth rate is expected to correspond to ice growth inhibition in real-world systems. In addition to presenting published simulation studies on the mechanism of ice growth inhibition by AFPs, this review also outlines the direction of future simulation studies in this field.

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Section: Fundamentals Of Afpsmentioning

confidence: 99%

Antifreeze proteins: computer simulation studies on the mechanism of ice growth inhibition

Nada

Furukawa

2012

Polym J

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“…Additionally, Parks & Lynch (1992) hypotethize that some sperm can present a high resistance to rapid cooling, this being probably related to the glycolipid components of the sperm membrane. Concerning this matter, there are studies that correlate certain proteins and glycoproteins, present in bodily fluids, to the maintenance of cell viability at low temperatures (Bouvet & Ben 2003, Davies et al 2002. Therefore, it is likely that the vulnerability of gametes subjected to cold temperatures, found in certain species, like armadillos, is associated to low concentrations or absence of such specific substances.…”

Section: Discussionmentioning

confidence: 99%

Identification of ultrastructural and functional damages in sperm from six-banded armadillos (Euphractus sexcinctus) due to cryopreservation

et al. 2016

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RESUMO.-[Identificação de danos ultraestruturais e funcionais em espermatozoides de tatus-peba (Euphractus sexcinctus) oriundos da criopreservação.] O objetivo deste estudo foi criopreservar o sêmen de tatus-peba (Euphractus sexcinctus) em diluente Tris-gema e glicerol, e determinar os danos causados pelo processo de congelação-descongelação, utilizando marcadores fluorescentes e análise ultraestrutural. As amostras de sêmen (n=11) coletadas de 4 tatus-peba adultos por eletroejaculação foram criopreservadas em diluente Tris acrescido de 20% de gema de ovo e 3% de glicerol, em curva rápida de congelação. A análise clássica das amostras foi realizada após a diluição, refrigeração e descongelação, seguida por análise de fluorescência, utilizando uma combinação de sondas flu- The aim of the study was to cryopreserve the semen of six-banded armadillos (Euphractus sexcinctus) in Tris-yolk and glycerol diluent, and to determine the damage caused by the freezing-thawing process, using fluorescent markers and ultrastructural analysis. Semen samples (n=11) collected from 4 adult six-banded armadillos by electroejaculation were cryopreserved in Tris diluent plus 20% egg yolk and 3% glycerol, in a fast freezing curve. Classical analysis of samples was performed after dilution, refrigeration and thawing, followed by fluorescence analysis, using a combination of fluorescent probes to assess membrane integrity (propidium iodide -PI and Hoechst -H342), and mitochondrial activity (CMXRos -Mito Tracker Red ® ). We also used the ultrastructural analysis to verify possible morphological alterations caused by cryoinjuries. When compared with fresh samples, we verified a significant decline in all the armadillos' semen parameters after thawing, in which only 6.1% motile sperm were found. However, the percentage of sperm which remained with viable (13%) and functional (24.7%) membranes after thawing suggests that some cells could be live but immotile. Analysis using fluorescent markers revealed that the mitochondria of armadillos' sperm is highly sensible to the freezing protocol and the findings through ultrastructure analysis proved this statement. Additionally, the images obtained by transmission electron microscopy revealed that frozen-thawed sperm presented damaged plasma membrane, nuclear modifications as changes in chromatin and acrossomal changes relative to sperm capacitation. In conclusion, this study is the first attempt to cryopreserve the semen of an armadillo species, and to help us to identify critical points on the freezing-thawing procedure in order to improve the protocol. Além disso, as imagens obtidas por microscopia eletrônica de transmissão revelaram que espermatozoides congelados-descongelados apresentaram membranas plasmáticas danificadas, modificações nucleares como alterações na cromatina, e alterações acrossomais relativas à capacitação espermática. Em conclusão, este estudo é a primeira tentativa de criopreservação de sêmen em uma espécie de tatu, e nos auxiliou a identificar pontos críticos no processo de ...

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“…AFPs bind to ice crystals and cause differences between the freezing point and melting point (TH: thermal hysteresis) through an adsorption-inhibition mechanism, thereby protecting organisms from ice damage (1)(2)(3). Broadly speaking, IBPs include AFPs and other ice-nucleating proteins.…”

mentioning

confidence: 99%

“…Although each antifreeze class differs dramatically in its sequences and structures and even binds to different planes of ice, the various classes do have some properties in common (2,3,26). The ice-binding sites are relatively hydrophobic and flat, which provide good surface-surface complementarity with the ice crystal.…”

mentioning

confidence: 99%

Structural Basis for Antifreeze Activity of Ice-binding Protein from Arctic Yeast

Lee

Park

et al. 2012

Journal of Biological Chemistry

122

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Background: Ice-binding proteins improve the cold tolerance of cells by inhibiting ice growth and recrystallization. Results: Crystal structure and mutagenesis data of LeIBP suggests the B face as an ice-binding site. Conclusion: LeIBP structure adopts a ␤-helical fold and the aligned Thr/Ser/Ala residues are critical for ice binding. Significance: LeIBP structure can serve as a structural model for a large number of IBPs.

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Structure and function of antifreeze proteins

Cited by 279 publications

References 35 publications

Antifreeze proteins: computer simulation studies on the mechanism of ice growth inhibition

Antifreeze proteins: computer simulation studies on the mechanism of ice growth inhibition

Identification of ultrastructural and functional damages in sperm from six-banded armadillos (Euphractus sexcinctus) due to cryopreservation

Structural Basis for Antifreeze Activity of Ice-binding Protein from Arctic Yeast

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