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Journal articles on the topic 'Ice recrystallization inhibitors'

Author: Grafiati
Published: 24 June 2021
Last updated: 8 February 2022

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1

William, Nishaka, and Jason Acker. "Modulating intracellular ice recrystallization in hepatocytes using small carbohydrate-based ice recrystallization inhibitors." Cryobiology 97 (December 2020): 258. http://dx.doi.org/10.1016/j.cryobiol.2020.10.040.

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2

William, Nishaka, Robert Ben, Jayan Nagendran, and Jason Acker. "Controlling Intra- And Extracellular Ice Recrystallization In Liver Tissues Using Small Molecule Ice Recrystallization Inhibitors." Cryobiology 91 (December 2019): 180–81. http://dx.doi.org/10.1016/j.cryobiol.2019.10.136.

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3

Poisson, J., T. Turner, A. Hill, J. P. Acker, and R. Ben. "Ice recrystallization inhibitors as novel cell-permeating cryoprotectants." Cryobiology 73, no. 3 (December 2016): 412. http://dx.doi.org/10.1016/j.cryobiol.2016.09.055.

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4

Meyer, J., J. Poisson, T. R. Turner, D. Burger, J. P. Acker, and R. Ben. "Investigating microparticle formation with novel ice recrystallization inhibitors." Cryobiology 73, no. 3 (December 2016): 428. http://dx.doi.org/10.1016/j.cryobiol.2016.09.114.

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5

Charlton, T. A., D. McCulloch, and R. N. Ben. "Sulfated alditol derivatives as novel ice recrystallization inhibitors." Cryobiology 73, no. 3 (December 2016): 436. http://dx.doi.org/10.1016/j.cryobiol.2016.09.144.

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6

Adam, Madeleine K., Jessica S. Poisson, Yingxue Hu, Geethika Prasannakumar, Matthew J. Pottage, Robert N. Ben, and Brendan L. Wilkinson. "Carbohydrate-based surfactants as photocontrollable inhibitors of ice recrystallization." RSC Advances 6, no. 45 (2016): 39240–44. http://dx.doi.org/10.1039/c6ra07030b.

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7

Poisson, Jessica S., Jason P. Acker, Jennie G. Briard, Julia E. Meyer, and Robert N. Ben. "Modulating Intracellular Ice Growth with Cell-Permeating Small-Molecule Ice Recrystallization Inhibitors." Langmuir 35, no. 23 (August 17, 2018): 7452–58. http://dx.doi.org/10.1021/acs.langmuir.8b02126.

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8

Balcerzak, Anna K., Michela Febbraro, and Robert N. Ben. "The importance of hydrophobic moieties in ice recrystallization inhibitors." RSC Advances 3, no. 10 (2013): 3232. http://dx.doi.org/10.1039/c3ra23220d.

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9

Adam, M. K., J. S. Poisson, Y. Hu, G. Prasannakumar, M. J. Pottage, B. L. Wilkinson, and R. N. Ben. "Carbohydrate-based surfactants as photocontrollable inhibitors of ice recrystallization." Cryobiology 73, no. 3 (December 2016): 436. http://dx.doi.org/10.1016/j.cryobiol.2016.09.143.

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10

Adam, Madeleine K., Yingxue Hu, Jessica S. Poisson, Matthew J. Pottage, Robert N. Ben, and Brendan L. Wilkinson. "Photoswitchable carbohydrate-based fluorosurfactants as tuneable ice recrystallization inhibitors." Carbohydrate Research 439 (February 2017): 1–8. http://dx.doi.org/10.1016/j.carres.2016.12.004.

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11

Tonelli, Devin, Chantelle J. Capicciotti, Malay Doshi, and Robert N. Ben. "Inhibiting gas hydrate formation using small molecule ice recrystallization inhibitors." RSC Advances 5, no. 28 (2015): 21728–32. http://dx.doi.org/10.1039/c4ra14746d.

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12

Balcerzak, Anna K., Chantelle J. Capicciotti, Jennie G. Briard, and Robert N. Ben. "Designing ice recrystallization inhibitors: from antifreeze (glyco)proteins to small molecules." RSC Adv. 4, no. 80 (2014): 42682–96. http://dx.doi.org/10.1039/c4ra06893a.

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13

Balcerzak, Anna K., Kyle McClymont, and Robert N. Ben. "140 The importance of hydrophobic moieties in ice recrystallization inhibitors." Cryobiology 67, no. 3 (December 2013): 438. http://dx.doi.org/10.1016/j.cryobiol.2013.09.146.

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14

Briard, Jennie G., Jessica S. Poisson, Tracey R. Turner, Jayme D. R. Kurach, Jason P. Acker, and Robert N. Ben. "Small molecule ice recrystallization inhibitors – A novel class of cryoprotectants." Cryobiology 71, no. 3 (December 2015): 540–41. http://dx.doi.org/10.1016/j.cryobiol.2015.10.018.

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15

Meyer, Julia E., Tracey R. Turner, Thomas A. Charlton, Jessica S. Poisson, Jason P. Acker, and Robert N. Ben. "Combining Ice Recrystallization Inhibitors To Improve Red Blood Cell Cryopreservation." Cryobiology 91 (December 2019): 163. http://dx.doi.org/10.1016/j.cryobiol.2019.10.074.

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16

Musca, V., and R. Ben. "Importance of the C1 heteroatom in aryl glycoside ice recrystallization inhibitors." Cryobiology 73, no. 3 (December 2016): 436–37. http://dx.doi.org/10.1016/j.cryobiol.2016.09.145.

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17

Turner, Tracey R., Jessica S. Poisson, Julia E. Meyer, Robert Ben, and Jason P. Acker. "Ice recrystallization inhibitors mitigate damage due to transient warming of cryopreserved RBCS." Cryobiology 85 (December 2018): 131. http://dx.doi.org/10.1016/j.cryobiol.2018.10.057.

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18

Poisson, Jessica S., Tracey R. Turner, Jason P. Acker, and Robert N. Ben. "Cryopreservation of red blood cells using ice recrystallization inhibitors as novel cryoprotectants." Cryobiology 85 (December 2018): 131–32. http://dx.doi.org/10.1016/j.cryobiol.2018.10.058.

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19

Mitchell, Daniel E., Mary Lilliman, Sebastian G. Spain, and Matthew I. Gibson. "Quantitative study on the antifreeze protein mimetic ice growth inhibition properties of poly(ampholytes) derived from vinyl-based polymers." Biomater. Sci. 2, no. 12 (2014): 1787–95. http://dx.doi.org/10.1039/c4bm00153b.

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Antifreeze (glyco) proteins (AF(G)Ps) from the blood of polar fish species are extremely potent ice recrystallization inhibitors (IRI), but are difficult to synthesise or extract from natural sources.
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20

Capicciotti, Chantelle J., Ross S. Mancini, Tracey R. Turner, Toshie Koyama, Matthew G. Alteen, Malay Doshi, Takaaki Inada, Jason P. Acker, and Robert N. Ben. "O-Aryl-Glycoside Ice Recrystallization Inhibitors as Novel Cryoprotectants: A Structure–Function Study." ACS Omega 1, no. 4 (October 24, 2016): 656–62. http://dx.doi.org/10.1021/acsomega.6b00163.

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21

Khan, S., J. Poisson, L. Davila, R. N. Ben, and D. W. Courtman. "Small-molecule ice recrystallization inhibitors improve post-thaw recovery of mesenchymal stromal cells." Cytotherapy 21, no. 5 (May 2019): S76. http://dx.doi.org/10.1016/j.jcyt.2019.03.477.

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22

Ben, Robert, Jennie G. Briard, Jessica S. Poisson, Tracey R. Turner, Jayme D. R. Kurach, and Jason P. Acker. "25. Ice recrystallization inhibitors – Mitigating cellular damage during freezing, transient warming and thawing." Cryobiology 71, no. 1 (August 2015): 171. http://dx.doi.org/10.1016/j.cryobiol.2015.05.031.

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23

Briard, Jennie, Jessica Poisson, Tracey Turner, Priya Chandran, Jason Acker, David Allan, and Robert Ben. "Carbohydrate-based small molecule ice recrystallization inhibitors as cryopreservatives for red blood cells." Cryobiology 71, no. 3 (December 2015): 554. http://dx.doi.org/10.1016/j.cryobiol.2015.10.072.

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24

Acker, Jason. "Application Of Small Molecule Ice Recrystallization Inhibitors In The Cryopreservation Of Cell Therapies." Cryobiology 91 (December 2019): 156. http://dx.doi.org/10.1016/j.cryobiol.2019.10.046.

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25

Raju, Rekha, Theresa Merl, Madeleine K. Adam, Emiliyan Staykov, Robert N. Ben, Gary Bryant, and Brendan L. Wilkinson. "n-Octyl (Thio)glycosides as Potential Cryoprotectants: Glass Transition Behaviour, Membrane Permeability, and Ice Recrystallization Inhibition Studies." Australian Journal of Chemistry 72, no. 8 (2019): 637. http://dx.doi.org/10.1071/ch19159.

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A series of eight n-octyl (thio)glycosides (1α, β–4α, β) with d-glucose or d-galactose-configured head groups and varying anomeric configuration were synthesized and evaluated for glass transition behaviour, membrane permeability, and ice recrystallization inhibition (IRI) activity. Of these, n-octyl β-d-glucopyranoside (2β) exhibited a high glass transition temperatures (Tg), both as a neat sample and 20 wt-% aqueous solution. Membrane permeability studies of this compound revealed cellular uptake to concentrations relevant to the inhibition of intracellular ice formation, thus presenting a promising lead candidate for further biophysical and cryopreservation studies. Compounds were also evaluated as ice recrystallization inhibitors; however, no detectable activity was observed for the newly tested compounds.
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26

Wang, Yannan, Laurie A. Graham, Zhifu Han, Robert Eves, Audrey K. Gruneberg, Robert L. Campbell, Heqiao Zhang, and Peter L. Davies. "Carrot ‘antifreeze’ protein has an irregular ice-binding site that confers weak freezing point depression but strong inhibition of ice recrystallization." Biochemical Journal 477, no. 12 (June 22, 2020): 2179–92. http://dx.doi.org/10.1042/bcj20200238.

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Ice-binding proteins (IBPs) are found in many biological kingdoms where they protect organisms from freezing damage as antifreeze agents or inhibitors of ice recrystallization. Here, the crystal structure of recombinant IBP from carrot (Daucus carota) has been solved to a resolution of 2.3 Å. As predicted, the protein is a structural homologue of a plant polygalacturonase-inhibiting protein forming a curved solenoid structure with a leucine-rich repeat motif. Unexpectedly, close examination of its surface did not reveal any large regions of flat, regularly spaced hydrophobic residues that characterize the ice-binding sites (IBSs) of potent antifreeze proteins from freeze-resistant fish and insects. An IBS was defined by site-directed mutagenesis of residues on the convex surface of the carrot solenoid. This imperfect site is reminiscent of the irregular IBS of grass ‘antifreeze’ protein. Like the grass protein, the carrot IBP has weak freezing point depression activity but is extremely active at nanomolar concentrations in inhibiting ice recrystallization. Ice crystals formed in the presence of both plant proteins grow slowly and evenly in all directions. We suggest that this slow, controlled ice growth is desirable for freeze tolerance. The fact that two plant IBPs have evolved very different protein structures to affect ice in a similar manner suggests this pattern of weak freezing point depression and strong ice recrystallization inhibition helps their host to tolerate freezing rather than to resist it.
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27

Abraham, Stephanie, Kerkeslin Keillor, Chantelle J. Capicciotti, G. Evan Perley-Robertson, Jeffrey W. Keillor, and Robert N. Ben. "Quantitative Analysis of the Efficacy and Potency of Novel Small Molecule Ice Recrystallization Inhibitors." Crystal Growth & Design 15, no. 10 (September 22, 2015): 5034–39. http://dx.doi.org/10.1021/acs.cgd.5b00995.

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28

Trant, John F., Robyn A. Biggs, Chantelle J. Capicciotti, and Robert N. Ben. "Developing highly active small molecule ice recrystallization inhibitors based upon C-linked antifreeze glycoprotein analogues." RSC Advances 3, no. 48 (2013): 26005. http://dx.doi.org/10.1039/c3ra43835j.

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29

Ben, Robert, Jessica Poisson, Jennie Briard, Tracey Turner, and Jason Acker. "Hydroxyethyl Starch Supplemented with Ice Recrystallization Inhibitors Greatly Improves Cryopreservation of Human Red Blood Cells." BioProcessing Journal 15, no. 4 (February 15, 2017): 16–21. http://dx.doi.org/10.12665/j154.ben.

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30

Turner, T., A. Hill, J. Briard, J. Poisson, R. Ben, and J. Acker. "Translating small molecule ice recrystallization inhibitors in the clinic: Establishing a large scale-up protocol." Cryobiology 73, no. 3 (December 2016): 402. http://dx.doi.org/10.1016/j.cryobiol.2016.09.019.

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31

Briard, Jennie G., Suria Jahan, Priya Chandran, David Allan, Nicolas Pineault, and Robert N. Ben. "Small-Molecule Ice Recrystallization Inhibitors Improve the Post-Thaw Function of Hematopoietic Stem and Progenitor Cells." ACS Omega 1, no. 5 (November 28, 2016): 1010–18. http://dx.doi.org/10.1021/acsomega.6b00178.

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32

Acker, Jason P., Chantelle J. Capicciotti, Jayme D. R. Kurach, Tracey R. Turner, Ross S. Mancini, and Robert N. Ben. "Small molecule ice recrystallization inhibitors enable freezing of human red blood cells with reduced glycerol concentrations." Transfusion Medicine Reviews 29, no. 4 (October 2015): 277. http://dx.doi.org/10.1016/j.tmrv.2015.05.005.

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33

Ben, Robert. "065 Designing potent inhibitors of Ice recrystallization - from C-linked antifreeze glycoproteins (AFGPs) to small molecules." Cryobiology 67, no. 3 (December 2013): 416. http://dx.doi.org/10.1016/j.cryobiol.2013.09.071.

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34

Capicciotti, Chantelle J., Jayme Tchir, Tracey Turner, Ross Mancini, Jason P. Acker, and Robert N. Ben. "067 Small carbohydrate-based molecules as potent ice recrystallization inhibitors and their application in red blood cell cryopreservation." Cryobiology 67, no. 3 (December 2013): 416. http://dx.doi.org/10.1016/j.cryobiol.2013.09.073.

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35

Lautner, Larissa, Robert N. Ben, Jason Acker, and Jayan Nagendran. "The Use Of Ice Recrystallization Inhibitors (Iris) In Pneumocyte Monolayer Cryopreservation To Reduce Cryoprotectant Toxicity, Control Intracellular Ice Growth And Improve Post-Thaw Survival." Cryobiology 91 (December 2019): 176. http://dx.doi.org/10.1016/j.cryobiol.2019.10.119.

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36

Chopra, Karishma, Salma Alasmar, Ahmed Zafer, Junzhuo Huang, Anna Jezierski, Scott Mccomb, Ewa Bauman, and Robert N. Ben. "Improving The Cryopreservation Of Human Induced Pluripotent Stem Cells (Ipscs) And Human T-Cells With Ice Recrystallization Inhibitors (Iris)." Cryobiology 91 (December 2019): 162. http://dx.doi.org/10.1016/j.cryobiol.2019.10.070.

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37

Lautner, Larissa, Jason Acker, and Jayan Nagendran. "Characterizing the efficacy of ice recrystallization inhibitors in rat lung cryopreservation using a low-cost subnormothermic ex vivo lung perfusion technique." Cryobiology 97 (December 2020): 271. http://dx.doi.org/10.1016/j.cryobiol.2020.10.088.

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38

Lautner, Larissa, Sayed Himmat, Jason P. Acker, and Jayan Nagendran. "The efficacy of ice recrystallization inhibitors in rat lung cryopreservation using a low cost technique for ex vivo subnormothermic lung perfusion." Cryobiology 97 (December 2020): 93–100. http://dx.doi.org/10.1016/j.cryobiol.2020.10.001.

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39

Pedchenko, Nazar, Ivan Zezekalo, Larysa Pedchenko, and Mykhailo Pedchenko. "Research into phase transformations in reservoir systems models in the presence of thermodynamic hydrate formation inhibitors of high concentration." E3S Web of Conferences 230 (2021): 01014. http://dx.doi.org/10.1051/e3sconf/202123001014.

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Gas hydrates have been and still remain a difficult problem in the oil and gas industry, solution of which requires considerable efforts and resources. In this work, the mechanism of phase transformations at negative temperatures in the formation of the solid phase is preliminarily studied using the reservoir system models consisting of a gas mixture and a solution of gas hydrate formation inhibitor of thermodynamic action with high concentration in distilled water. A system of three-dimensional lighting and image magnification is used to visually detect phase boundaries by creating optical effects. Thus, in the system “inhibitor solution – gas hydrate – gas” in the process of gas hydrate recrystallization in the conditions close to equilibrium, microzones of supercooled water may occur, which in the absence of gas molecules access is crystallized into ice. The result of such solid phase structure formation is its increased stability in nonequilibrium conditions for a relatively long period of time.
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40

Six, Katrijn R., Stijn Lyssens, Rosalie Devloo, Veerle Compernolle, and Hendrik B. Feys. "The ice recrystallization inhibitor polyvinyl alcohol does not improve platelet cryopreservation." Transfusion 59, no. 9 (September 2019): 3029–31. http://dx.doi.org/10.1111/trf.15395.

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41

Waters, Lauren, Robert Ben, Jason P. Acker, Matthew P. Padula, Denese C. Marks, and Lacey Johnson. "Characterizing the ability of an ice recrystallization inhibitor to improve platelet cryopreservation." Cryobiology 96 (October 2020): 152–58. http://dx.doi.org/10.1016/j.cryobiol.2020.07.003.

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42

Briard, Jennie G., Michael Fernandez, Phil De Luna, Tom K. Woo, and Robert N. Ben. "QSAR Accelerated Discovery of Potent Ice Recrystallization Inhibitors." Scientific Reports 6, no. 1 (May 24, 2016). http://dx.doi.org/10.1038/srep26403.

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43

Ghobadloo, Shahrokh M., Anna K. Balcerzak, Ana Gargaun, Darija Muharemagic, Gleb G. Mironov, Chantelle J. Capicciotti, Jennie G. Briard, Robert N. Ben, and Maxim V. Berezovski. "Carbohydrate-Based Ice Recrystallization Inhibitors Increase Infectivity and Thermostability of Viral Vectors." Scientific Reports 4, no. 1 (July 31, 2014). http://dx.doi.org/10.1038/srep05903.

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44

Provesi, João Gustavo, Pedro Alexandre Valentim Neto, Ana Carolina Maisonnave Arisi, and Edna Regina Amante. "Antifreeze proteins in naturally cold acclimated leaves of Drimys angustifolia, Senecio icoglossus, and Eucalyptus ssp." Brazilian Journal of Food Technology 19 (2016). http://dx.doi.org/10.1590/1981-6723.11016.

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Summary Antifreeze proteins (AFPs) present in plants may inhibit ice recrystallization even at low concentrations, and show potential application to many frozen foods. This study evaluated the presence of antifreeze proteins in naturally cold acclimated and non-acclimated leaves of Drimys angustifolia, Senecio icoglossus and Eucalyptus ssp. No proteins were detected in apoplastic extracts of Eucalyptus ssp. Extracts of cold acclimated and non-acclimated S. icoglossus showed protein concentrations of 42.89 and 17.76 µg mL-1, both with bands between 25 and 37 kDa in the SDS-PAGE. However, they did not inhibit recrystallization. The extract of cold acclimated D. angustifolia contained a protein concentration of 95.17 µg mL-1, almost five times higher than the extract of non-acclimated D. angustifolia. In the extract of cold acclimated D. angustifolia, there was presence of ice recrystallization inhibitors. This extract showed a protein band just below 37 kDa and another more intense band between 20 and 25 kDa. It is the first time that the presence of antifreeze proteins in this species is being described.
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45

Capicciotti, Chantelle J., Jayme D. R. Kurach, Tracey R. Turner, Ross S. Mancini, Jason P. Acker, and Robert N. Ben. "Small Molecule Ice Recrystallization Inhibitors Enable Freezing of Human Red Blood Cells with Reduced Glycerol Concentrations." Scientific Reports 5, no. 1 (April 8, 2015). http://dx.doi.org/10.1038/srep09692.

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46

Briard, Jennie G., Jessica S. Poisson, Tracey R. Turner, Chantelle J. Capicciotti, Jason P. Acker, and Robert N. Ben. "Small molecule ice recrystallization inhibitors mitigate red blood cell lysis during freezing, transient warming and thawing." Scientific Reports 6, no. 1 (March 29, 2016). http://dx.doi.org/10.1038/srep23619.

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47

"Study of polyvinyl alcohols (9 and 31 kDa) aggregation in aqueous solutions by fluorescent probing." Biophysical Bulletin, no. 44 (2020). http://dx.doi.org/10.26565/2075-3810-2020-44-01.

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Background: When developing low-temperature cell storage methods, a serious problem is recrystallization, which leads to cell damage during thawing. Previous studies have shown the promising use of polyvinyl alcohol (PVA) as an inhibitor of recrystallization. But the mechanisms of protective action of PVA are not finally clarified. So, it is not known what structural features contribute to implementation of PVA antirecrystallization properties in the cryoprotective concentration range. Objectives: Establishing the peculiarities of structuring PVA molecules in aqueous solutions using the fluorescent probe. Materials and Methods: Aqueous solutions of 0.1–5% (wt.%) PVA with molecular mass (m.m.) of 9 and 31 kDa) were studied. Fluorescence probe method, photometry, stalagmometry, and molecular modeling were used. Results: Using the 3-hydroxy-4¢-(N,N-dimethylamino)flavones (FME) fluorescent probe it was found that in 0.1–5% of PVA (m.m. 9 and 31 kDa) aqueous solutions the structural organization of polymers changes with formation of different in size and structure of local hydrophobic regions. In PVA solutions, m.m. 9 kDa micelles with smaller cavities are formed in which FME is densely surrounded by polymer segments. In the case of PVA m.m. 31 kDa, it forms micelles with smaller cavities surrounded by polymer segments. PVA m.m. 31 kDa forms micelles with larger in size and more hydrophilic cavities. If the content is more than 3%, PVA m.m. 31 kDa aggregates are partially destroyed, which may be the result of increased water content. Under these conditions, PVA m.m. 9 kDa micelles are enlarged. as a result of aggregation. According to molecular modeling data, PVA is able to form strong hydrogen-linked complexes with the surface of ice nanocrystals. Such complex, having a hydrophobic surface, can depolarize water molecules, thus slowing down further growth of ice crystals. Conclusions: Changes in the structural organization, which may affect the recrystallization properties, have been found in water solutions of PVA. The mechanism of implementation of polymer anticrystallization activity has been suggested. The possible role of structure and supramolecular organization of PVA in aqueous solutions in understanding the mechanisms of depressing recrystallization during freeze-thawing of cells is discussed.
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