The Experts below are selected from a list of 258 Experts worldwide ranked by ideXlab platform
Choy L. Hew - One of the best experts on this subject based on the ideXlab platform.
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Aggregation of Antifreeze protein and impact on Antifreeze activity.
The Journal of Physical Chemistry B, 2006Co-Authors: Xiang-yang Liu, Choy L. HewAbstract:Antifreeze protein type III aggregates once the concentration exceeds a critical value, the so-called critical aggregation concentration (CAC). It was found for the first time that the aggregation of Antifreeze protein exerts a direct impact on the Antifreeze efficiency. It follows from our measurements that the AFP III above CAC will enhance the Antifreeze activity because of the increase of the kink kinetics barrier of surface integration. This is attributed to the optimal packing of AFP III molecules on the surface of the ice nucleus as well as ice crystals above CAC. This study will extend our understanding of the Antifreeze mechanism of Antifreeze protein monomers as well as Antifreeze aggregates on ice nucleation and shed light on the selection of Antifreeze agents.
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Ice nucleation inhibition: mechanism of Antifreeze by Antifreeze protein.
Journal of Biological Chemistry, 2003Co-Authors: Xiang-yang Liu, Choy L. HewAbstract:The effect of Antifreeze protein type III (one type of fish Antifreeze protein) on ice crystallization was examined quantitatively based on a "micro-sized ice nucleation" technique. It was found for the first time that Antifreeze proteins can inhibit the ice nucleation process by adsorbing onto both the surfaces of ice nuclei and dust particles. This leads to an increase of the ice nucleation barrier and the desolvation kink kinetics barrier, respectively. Based on the latest nucleation model, the increases in the ice nucleation barrier and the kink kinetics barrier were measured. This enables us to quantitatively examine the Antifreeze mechanism of Antifreeze proteins for the first time.
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Fish Antifreeze Proteins - Fish Antifreeze proteins
Molecular Aspects of Fish & Marine Biology, 2002Co-Authors: Kathryn Vanya Ewart, Choy L. HewAbstract:Early research on proteins from the Antarctic - Antifreeze glycoproteins, R.A. Feeney and D.T. Osuga physiological ecology of Antifreeze proteins - a northern perspective, S.V. Goddard and G.L. Fletcher fish Antifreeze proteins - functions, molecular interactions and biological roles, K.V. Ewart origins and evolution of fish Antifreeze proteins, C.C.-M. Cheng and A.L. DeVries the structure of fish Antifreeze proteins, D.J. Brown and F.D. Sonnichsen control of Antifreeze protein gene expression in winter flounder, M. Miao et al the skin-type Antifreeze polypeptides - a new class of type I AFPs, W.-K. Low et al the interaction of Antifreeze proteins with model membranes and cells, M.M. Tomczak and J.H. Crowe Antifreeze protein gene transfer in salmonids, W.-K. Low et al.
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Low-temperature increases the yield of biologically active herring Antifreeze protein in Pichia pastoris.
Protein Expression and Purification, 2001Co-Authors: Fei Xiong, Daniel S C Yang, Qingsong Lin, Marc C. D'anjou, Andrew J. Daugulis, Choy L. HewAbstract:Abstract Antifreeze proteins and Antifreeze glycoproteins are structurally diverse molecules that share a common property in binding to ice crystals and inhibiting ice crystal growth. Type II fish Antifreeze protein of Atlantic herring ( Clupea harengus harengus ) is unique in its requirement of Ca 2+ for Antifreeze activity. In this study, we utilized the secretion vector pGAPZα A to express recombinant herring Antifreeze protein (WT) and a fusion protein with a C-terminal six-histidine tag (WT-6H) in yeast Pichia pastoris wild-type strain X-33 or protease-deficient strain SMD1168H. Both recombinant proteins were secreted into the culture medium and properly folded and functioned as the native herring Antifreeze protein. Furthermore, our studies demonstrated that expression at a lower temperature increased the yield of the recombinant protein dramatically, which might be due to the enhanced protein folding pathway, as well as increased cell viability at lower temperature. These data suggested that P. pastoris is a useful system for the production of soluble and biologically active herring Antifreeze protein required for structural and functional studies.
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Structure, function and evolution of Antifreeze proteins
Cellular and molecular life sciences : CMLS, 1999Co-Authors: Kathryn Vanya Ewart, Qingsong Lin, Choy L. HewAbstract:Antifreeze proteins bind to ice crystals and modify their growth. These proteins show great diversity in structure, and they have been found in a variety of organisms. The ice-binding mechanisms of Antifreeze proteins are not completely understood. Recent findings on the evolution of Antifreeze proteins and on their structures and mechanisms of action have provided new understanding of these proteins in different contexts. The purpose of this review is to present the developments in contrasting research areas and unite them in order to gain further insight into the structure and function of the Antifreeze proteins.
Arthur L Devries - One of the best experts on this subject based on the ideXlab platform.
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blocking rapid ice crystal growth through nonbasal plane adsorption of Antifreeze proteins
Proceedings of the National Academy of Sciences of the United States of America, 2016Co-Authors: Luuk L C Olijve, Konrad Meister, Arthur L Devries, John G. Duman, Huib J Bakker, Ilja K. VoetsAbstract:Antifreeze proteins (AFPs) are a unique class of proteins that bind to growing ice crystal surfaces and arrest further ice growth. AFPs have gained a large interest for their use in Antifreeze formulations for water-based materials, such as foods, waterborne paints, and organ transplants. Instead of commonly used colligative Antifreezes such as salts and alcohols, the advantage of using AFPs as an additive is that they do not alter the physicochemical properties of the water-based material. Here, we report the first comprehensive evaluation of thermal hysteresis (TH) and ice recrystallization inhibition (IRI) activity of all major classes of AFPs using cryoscopy, sonocrystallization, and recrystallization assays. The results show that TH activities determined by cryoscopy and sonocrystallization differ markedly, and that TH and IRI activities are not correlated. The absence of a distinct correlation in Antifreeze activity points to a mechanistic difference in ice growth inhibition by the different classes of AFPs: blocking fast ice growth requires rapid nonbasal plane adsorption, whereas basal plane adsorption is only relevant at long annealing times and at small undercooling. These findings clearly demonstrate that biomimetic analogs of Antifreeze (glyco)proteins should be tailored to the specific requirements of the targeted application.
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Antifreeze glycoprotein activity correlates with long range protein water dynamics
Journal of the American Chemical Society, 2010Co-Authors: Simon Ebbinghaus, Konrad Meister, Arthur L Devries, Benjamin Born, Martin Gruebele, Martina HavenithAbstract:Antifreeze proteins (AFPs) and Antifreeze glycoproteins (AFGPs) enable the survival of organisms living in subfreezing habitats and serve as preservatives. Although their function is known, the underlying molecular mechanism was not understood. Mutagenesis experiments questioned the previous assumption of hydrogen bonding as the dominant mechanism. We use terahertz spectroscopy to show that Antifreeze activity is directly correlated with long-range collective hydration dynamics. Our results provide evidence for a new model of how AFGPs prevent water from freezing. We suggest that Antifreeze activity may be induced because the AFGP perturbs the aqueous solvent over long distances. Retarded water dynamics in the large hydration shell does not favor freezing. The complexation of the carbohydrate cis-hydroxyl groups by borate suppresses the long-range hydration shell detected by terahertz absorption. The hydration dynamics shift toward bulk water behavior strongly reduces the AFGP Antifreeze activity, further supporting our model.
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Structure-Function Studies of Native and Recombinant Fish Antifreeze Proteins.
2000Co-Authors: Chi-hing C. Cheng-devries, Arthur L DevriesAbstract:Abstract : This project investigates the structures of several fish Antifreeze proteins, and how they interact with ice crystals and inhibit ice growth. Formation of hexagonal pit formation on ice crystal basal plane in the presence of fish Antifreeze proteins was examined with two-photon fluorescence imaging which showed binding of Antifreeze glycoproteins molecules on pit faces; the origin of pit development presumably stems from Antifreeze adsorption on dislocations on the basal plane. A novel ice-active protein was isolated from AFGP-bearing notothenioid fish and its partial structure was determined. This protein and AFGP together lead to synergistic augmentation of Antifreeze activity and thus has potential bearing on the design of more potent anti-freezing systems. A putative new type of Antifreeze peptide was isolated from an Arctic liparid fish and its partial sequence was determined. And lastly, the X-ray crystallographic structure of a type III Antifreeze peptide from an Antarctic eel pout and the protein's ice-binding surface were determined.
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Calorimetric analysis of Antifreeze glycoproteins of the polar fish, Dissostichus mawsoni.
Biochimica et biophysica acta, 1991Co-Authors: Thomas N. Hansen, Arthur L Devries, John G. BaustAbstract:Solutions of Antifreeze glycoproteins 1 through 5 and 8 were analyzed for activity by differential scanning calorimetry. With a scan rate of 1°C min −1 , Antifreeze glycoproteins 1–5 (20 mg/ml) revealed Antifreeze activity with a delay in the freeze exotherm during cooling in the presence of ice. Antifreeze glycoprotein 8 (60 mg/ml), however, did not reveal Antifreeze activity. When a 0.1°C min −1 scan rate was used, glycoproteins 1–5 again yielded a delay in the freeze onset, but the exotherm consisted of multiple events. At the slower scan glycoprotein 8 revealed an initial freeze followed by multiple exothermic events resembling those of glycoproteins 1–5. Thermograms exhibiting Antifreeze activity had an initial shoulder in the exotherm direction upon cooling followed by a delay before the exotherm. The shoulders were correlated with c -axis-formula> ice growth observed in visual methods. The glycoprotein Antifreezes had a linear increase in activity with decreased ice content.
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adsorption of alpha helical Antifreeze peptides on specific ice crystal surface planes
Biophysical Journal, 1991Co-Authors: Charles A. Knight, C Christina H Cheng, Arthur L DevriesAbstract:The noncolligative peptide and glycopeptide Antifreezes found in some cold-water fish act by binding to the ice surface and preventing crystal growth, not by altering the equilibrium freezing point of the water. A simple crystal growth and etching technique allows determination of the crystallographic planes where the binding occurs. In the case of elongated molecules, such as the alpha-helical peptides in this report, it also allows a deduction of the molecular alignment on the ice surface. The structurally similar Antifreeze peptides from winter flounder (Pseudopleuronectes americanus) and Alaskan plaice (Pleuronectes quadritaberulatus) adsorb onto the (2021) pyramidal planes of ice, whereas the sculpin (Myoxocephalus scorpius) peptide adsorbs on (2110), the secondary prism planes. All three are probably aligned along (0112). These Antifreeze peptides have 11-amino acid sequence repeats ending with a polar residue, and each repeat constitutes a distance of 16.5 A along the helix, which nearly matches the 16.7 A repeat spacing along (0112) in ice. This structural match is undoubtedly important, but the mechanism of binding is not yet clear. The suggested mechanism of growth inhibition operates through the influence of local surface curvature upon melting point and results in complete inhibition of the crystal growth even though individual Antifreeze molecules bind at only one interface orientation.
John G. Duman - One of the best experts on this subject based on the ideXlab platform.
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blocking rapid ice crystal growth through nonbasal plane adsorption of Antifreeze proteins
Proceedings of the National Academy of Sciences of the United States of America, 2016Co-Authors: Luuk L C Olijve, Konrad Meister, Arthur L Devries, John G. Duman, Huib J Bakker, Ilja K. VoetsAbstract:Antifreeze proteins (AFPs) are a unique class of proteins that bind to growing ice crystal surfaces and arrest further ice growth. AFPs have gained a large interest for their use in Antifreeze formulations for water-based materials, such as foods, waterborne paints, and organ transplants. Instead of commonly used colligative Antifreezes such as salts and alcohols, the advantage of using AFPs as an additive is that they do not alter the physicochemical properties of the water-based material. Here, we report the first comprehensive evaluation of thermal hysteresis (TH) and ice recrystallization inhibition (IRI) activity of all major classes of AFPs using cryoscopy, sonocrystallization, and recrystallization assays. The results show that TH activities determined by cryoscopy and sonocrystallization differ markedly, and that TH and IRI activities are not correlated. The absence of a distinct correlation in Antifreeze activity points to a mechanistic difference in ice growth inhibition by the different classes of AFPs: blocking fast ice growth requires rapid nonbasal plane adsorption, whereas basal plane adsorption is only relevant at long annealing times and at small undercooling. These findings clearly demonstrate that biomimetic analogs of Antifreeze (glyco)proteins should be tailored to the specific requirements of the targeted application.
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A thermal hysteresis-producing xylomannan glycolipid Antifreeze associated with cold tolerance is found in diverse taxa
Journal of Comparative Physiology B, 2011Co-Authors: Kent R. Walters, Todd Sformo, Anthony S. Serianni, Brian M Barnes, Yann Voituron, John G. DumanAbstract:The presence of large-molecular-mass, thermal hysteresis (TH)-producing Antifreezes (e.g., Antifreeze proteins) has been reported in numerous and diverse taxa, including representative species of fish, arthropods, plants, fungi, and bacteria. However, relatively few of these Antifreeze molecules have been chemically characterized. We screened diverse species by subjecting their homogenates to ice-affinity purification and discovered the presence of a newly identified class of Antifreeze, a xylomannan-based TH-producing glycolipid that was previously reported in one species of freeze-tolerant Alaskan beetle. We isolated xylomannan-based Antifreeze glycolipids from one plant species, six insect species, and the first frog species to be shown to produce a large-molecular-mass Antifreeze. ^1H NMR spectra of the ice-purified molecules isolated from these diverse freeze-tolerant and freeze-avoiding organisms were nearly identical, indicating that the chemical structures of the glycolipids were highly similar. Although the exact functions remain uncertain, it appears that Antifreeze glycolipids play a role in cold tolerance.
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a nonprotein thermal hysteresis producing xylomannan Antifreeze in the freeze tolerant alaskan beetle upis ceramboides
Proceedings of the National Academy of Sciences of the United States of America, 2009Co-Authors: Kent R. Walters, Todd Sformo, Anthony S. Serianni, Brian M Barnes, John G. DumanAbstract:Thermal hysteresis (TH), a difference between the melting and freezing points of a solution that is indicative of the presence of large-molecular-mass Antifreezes (e.g., Antifreeze proteins), has been described in animals, plants, bacteria, and fungi. Although all previously described TH-producing biomolecules are proteins, most thermal hysteresis factors (THFs) have not yet been structurally characterized, and none have been characterized from a freeze-tolerant animal. We isolated a highly active THF from the freeze-tolerant beetle, Upis ceramboides, by means of ice affinity. Amino acid chromatographic analysis, polyacrylamide gel electrophoresis, UV-Vis spectrophotometry, and NMR spectroscopy indicated that the THF contained little or no protein, yet it produced 3.7 ± 0.3 °C of TH at 5 mg/ml, comparable to that of the most active insect Antifreeze proteins. Compositional and structural analyses indicated that this Antifreeze contains a β-mannopyranosyl-(1→4) β-xylopyranose backbone and a fatty acid component, although the lipid may not be covalently linked to the saccharide. Consistent with the proposed structure, treatment with endo-β-(1→4)xylanase ablated TH activity. This xylomannan is the first TH-producing Antifreeze isolated from a freeze-tolerant animal and the first in a new class of highly active THFs that contain little or no protein.
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Enhancement of insect Antifreeze protein activity by antibodies.
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991Co-Authors: John G. DumanAbstract:Abstract Antifreeze proteins, produced by many cold water marine teleost fish and terrestrial arthropods (insects, spiders, etc.), inhibit ice crystal growth by a non-colligative mechanism, probably by adsorbing onto the surface of potential seed ice crystals and thereby blocking growth at preferred growth sites. In this study it is demonstrated that the activity of two insect Antifreeze proteins is greatly increased by the addition of specific rabbit polyclonal antibodies to the Antifreezes. A model is presented which suggests that the enhancement occurs because the Antifreeze-antibody complex, being much larger than the Antifreeze protein alone (a minimal 7–8-fold increase in size), blocks a larger area of the ice crystal surface and extends further above the surface, thus requiring the temperature to be further lowered before crystal growth proceeds. This idea is further supported by the finding that addition of goat anti-rabbit IgG to the Antifreeze protein + anti-Antifreeze protein antibody complexes further enhanced activity.
Marilyn Griffith - One of the best experts on this subject based on the ideXlab platform.
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Characterization of Antifreeze activity in Antarctic plants
Journal of experimental botany, 2005Co-Authors: León A. Bravo, Marilyn GriffithAbstract:Deschampsia antarctica and Colobanthus quitensis are the only vascular plants to have colonized the Maritime Antarctic, which is characterized by its permanently low temperature and frequent summer frosts. To understand how the plants survive freezing temperatures year-round, Antifreeze activity was assayed in apoplastic extracts obtained from both non-acclimated and cold-acclimated Antarctic plants. By observing the shape of ice crystals grown in dilution series of the extracts, it was found that D. antarctica had Antifreeze activity, but C. quitensis did not. D. antarctica exhibited Antifreeze activity in the non-acclimated state and this activity increased after cold acclimation. The Antifreeze activity in D. antarctica was labile to proteolysis and high temperature, active over a wide pH range, and associated with molecules greater than 10 kDa in molecular weight. These results show that D. antarctica produces Antifreeze proteins that are secreted into the apoplast. When examined by SDS-PAGE, the apoplastic extracts from cold-acclimated D. antarctica exhibited 13 polypeptides. It is concluded that D. antarctica accumulates AFPs as part of its mechanism of freezing tolerance. Moreover, this is the first plant in which Antifreeze activity has been observed to be constitutive.
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Antifreeze proteins in overwintering plants: a tale of two activities
Trends in plant science, 2004Co-Authors: Marilyn Griffith, Mahmoud W. YaishAbstract:Antifreeze proteins are found in a wide range of overwintering plants where they inhibit the growth and recrystallization of ice that forms in intercellular spaces. Unlike Antifreeze proteins found in fish and insects, plant Antifreeze proteins have multiple, hydrophilic ice-binding domains. Surprisingly, Antifreeze proteins from plants are homologous to pathogenesis-related proteins and also provide protection against psychrophilic pathogens. In winter rye ( Secale cereale ), Antifreeze proteins accumulate in response to cold, short daylength, dehydration and ethylene, but not pathogens. Transferring single genes encoding Antifreeze proteins to freezing-sensitive plants lowered their freezing temperatures by ∼1°C. Genes encoding dual-function plant Antifreeze proteins are excellent models for use in evolutionary studies to determine how genes acquire new expression patterns and how proteins acquire new activities.
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Ethylene Induces Antifreeze Activity in Winter Rye Leaves
Plant physiology, 2001Co-Authors: Marilyn Griffith, Steven B. WisemanAbstract:Antifreeze activity is induced by cold temperatures in winter rye (Secale cereale) leaves. The activity arises from six Antifreeze proteins that accumulate in the apoplast of winter rye leaves during cold acclimation. The individual Antifreeze proteins are similar to pathogenesis-related proteins, including glucanases, chitinases, and thaumatin-like proteins. The objective of this study was to study the regulation of Antifreeze activity in response to ethylene and salicyclic acid, which are known regulators of pathogenesis-related proteins induced by pathogens. Nonacclimated plants treated with salicylic acid accumulated apoplastic proteins with no Antifreeze activity. In contrast, when nonacclimated plants were exposed to ethylene, both Antifreeze activity and the concentration of apoplastic protein increased in rye leaves. Immunoblotting revealed that six of the seven accumulated apoplastic proteins consisted of two glucanases, two chitinases, and two thaumatin-like proteins. The ethylene-releasing agent ethephon and the ethylene precursor 1-aminocyclopropane-1-carboxylate also induced high levels of Antifreeze activity at 20 degrees C, and this effect could be blocked by the ethylene inhibitor AgNO(3). When intact rye plants were exposed to 5 degrees C, endogenous ethylene production and Antifreeze activity were detected within 12 and 48 h of exposure to cold, respectively. Rye plants exposed to drought produced both ethylene and Antifreeze activity within 24 h. We conclude that ethylene is involved in regulating Antifreeze activity in winter rye in response to cold and drought.
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Antifreeze proteins in winter rye
Physiologia Plantarum, 1997Co-Authors: Marilyn Griffith, Mervi Antikainen, Wai-ching Hon, Kaarina Pihakaski-maunsbach, Jong Un Chun, Daniel S C YangAbstract:Six Antifreeze proteins, which have the unique ability to adsorb onto the surface of ice and inhibit its growth, have been isolated from the apoplast of winter rye leaves where ice forms at subzero temperatures. The rye Antifreeze proteins accumulate during cold acclimation and are similar to plant pathogenesis-related proteins, including two endoglucanase-like, two chitinase-like and two thaumatin-like proteins. Immunolocalization of the glucanase-like Antifreeze proteins showed that they accumulate in mesophyll cell walls facing intercellular spaces, in pectinaceous regions between adjoining mestome sheath cells, in the secondary cell walls of xylem vessels and in epidermal cell walls. Because the rye Antifreeze proteins are located in areas where they could be in contact with ice, they may function as a barrier to the propagation of ice or to inhibit the recrystallization of ice. Antifreeze proteins similar to pathogenesis-related proteins were also found to accumulate in closely-related plants within the Triticum group but not in freezing-tolerant dicotyledonous plants. In winter wheat, the accumulation of Antifreeze proteins and the development of freezing tolerance are regulated by chromosome 5. Rye Antifreeze proteins may have evolved from pathogenesis-related proteins, but they retain their catalytic activities and may play a dual role in increasing both freezing and disease resistance in overwintering plants.
Ji Ma - One of the best experts on this subject based on the ideXlab platform.
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Cloning, sequencing and prokaryotic expression of cDNAs for Antifreeze protein family from beetle Tenebrio molitor
Frontiers of Biology in China, 2008Co-Authors: Zhongyuan Liu, Fu-chun Zhang, Guo-dong Lu, Xian-lei Wang, Yun Wang, Ji MaAbstract:Partial cDNA sequences coding for Antifreeze proteins in Tenebrio molitor were obtained by RT-PCR. Sequence analysis revealed nine putative cDNAs with a high degree of homology to Tenebrio molitor Antifreeze protein genes published in GenBank. The recombinant pGEX-4T-1-tmafp-XJ430 was introduced into E. coli BL21 to induce a GST fusion protein by IPTG. SDSPAGE analysis for the fusion protein shows a band of 38 kDa. pCDNA3-tmafp-XJ430 was injected into mice to generate antiserum which was later detected by indirect ELISA. The titer of the antibody was 1:2000.Western blotting analysis shows that the antiserum was specifically against the Antifreeze protein. Our results laid the foundation for further studies on the properties and functions of insect Antifreeze proteins.
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Cloning, sequencing and prokaryotic expression of cDNAs for the Antifreeze protein family from the beetle Tenebrio molitor
Hereditas, 2006Co-Authors: Zhongyuan Liu, Fu-chun Zhang, Guo-dong Lu, Xian-lei Wang, Yun Wang, Ji MaAbstract:The partial cDNA sequence coding for the Antifreeze proteins in the Tenebrio molitor was obtained by RT-PCR. Sequence analysis revealed nine putative cDNAs with a high degree of homology to Tenebrio molitor Antifreeze proteins. The recombinant pGEX-4T-1-tmafp-XJ430 was introduced into E. coli BL21 to induce a GST fusion protein by IPTG. SDS-PAGE of the fusion protein demonstrated that the Antifreeze protein migrated at a size of 38 kDa. The immunization was performed by intra-muscular injection of pCDNA3- tmafp-XJ430, and then antiserum was detected by ELISA.The titer of the antibody was 1:2 000. Western blotting analysis showed the antiserum was specific against the Antifreeze protein. This finding could lead to further investigation of the properties and function of Antifreeze proteins.