Ice Recrystallization Inhibition Using <scp>l</scp>-Alanine/<scp>l</scp>-Lysine Copolymers

Park, Soyeon; Piao, Zhengyu; Park, Jin Kyung; Lee, Hyun Jung; Jeong, Byeongmoon

doi:10.1021/acsapm.2c00174

Cited by 8 publications

(10 citation statements)

References 70 publications

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“…In 2017, Gibson and co-workers explored how short polyprolines, rather than poly(hydroxyprolines) (which when bought commercially can actually contain significant polyproline content), could lead to activity, supporting the emerging hypothesis that hydrophobic faces (rather than hydroxyls) engage ice in many IBPs . Although the oligoprolines were relatively weak in terms of IRI (not inhibiting all ice growth even at 20 mg mL –1 ), they were found useful for cryopreservation. , It is important to note that this is distinct from the effect of the amino acid l -proline in cryopreservation as a protective osmolyte. , Alanine/lysine copolymers have also been reported to show IRI activity; , for biomedical applications, the net cationic charge may lead to cytotoxicity. Poly(serine) has been tested for IRI, but the magnitude reported was essentially identical with a negative control of PEG .…”

Section: Introductionmentioning

confidence: 98%

High Molecular Weight Polyproline as a Potential Biosourced Ice Growth Inhibitor: Synthesis, Ice Recrystallization Inhibition, and Specific Ice Face Binding

Judge¹,

Georgiou

Bissoyi

et al. 2023

Biomacromolecules

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Ice-binding proteins (IBPs) from extremophile organisms can modulate ice formation and growth. There are many (bio)technological applications of IBPs, from cryopreservation to mitigating freeze–thaw damage in concrete to frozen food texture modifiers. Extraction or expression of IBPs can be challenging to scale up, and hence polymeric biomimetics have emerged. It is, however, desirable to use biosourced monomers and heteroatom-containing backbones in polymers for in vivo or environmental applications to allow degradation. Here we investigate high molecular weight polyproline as an ice recrystallization inhibitor (IRI). Low molecular weight polyproline is known to be a weak IRI. Its activity is hypothesized to be due to the unique PPI helix it adopts, but it has not been thoroughly investigated. Here an open-to-air aqueous N-carboxyanhydride polymerization is employed to obtain polyproline with molecular weights of up to 50000 g mol–1. These polymers were found to have IRI activity down to 5 mg mL–1, unlike a control peptide of polysarcosine, which did not inhibit all ice growth at up to 40 mg mL–1. The polyprolines exhibited lower critical solution temperature behavior and assembly/aggregation observed at room temperature, which may contribute to its activity. Single ice crystal assays with polyproline led to faceting, consistent with specific ice-face binding. This work shows that non-vinyl-based polymers can be designed to inhibit ice recrystallization and may offer a more sustainable or environmentally acceptable, while synthetically scalable, route to large-scale applications.

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Section: Introductionmentioning

confidence: 98%

High Molecular Weight Polyproline as a Potential Biosourced Ice Growth Inhibitor: Synthesis, Ice Recrystallization Inhibition, and Specific Ice Face Binding

Judge¹,

Georgiou

Bissoyi

et al. 2023

Biomacromolecules

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“…PATs-3 and PATs-4 exhibited higher IRI activity, suggesting that the alanine content or hydrophobic interactions participate in the IRI activity. Typically, introducing hydrophobic groups to a molecule increases the IRI activity. − IRI activity exhibited the following order: l -Ala < l -Val < l -Leu< l -Phe, proportional to the hydrophobicity of amino acids . In addition, poly( l -alanine- co - l -lysine) IRI activity and l -alanine content increased concurrently .…”

Section: Resultsmentioning

confidence: 99%

“…Typically, introducing hydrophobic groups to a molecule increases the IRI activity. − IRI activity exhibited the following order: l -Ala < l -Val < l -Leu< l -Phe, proportional to the hydrophobicity of amino acids . In addition, poly( l -alanine- co - l -lysine) IRI activity and l -alanine content increased concurrently . When graphene was functionalized with methyl, hydroxyl, and carboxylic acid groups, the IRI activity decreased in the following order: methyl>hydroxyl>carboxylic acid .…”

Section: Resultsmentioning

confidence: 99%

Poly(l-alanine-co-l-threonine succinate) as a Biomimetic Cryoprotectant

Park,

Jeong

2023

ACS Appl. Mater. Interfaces

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“…However, new compounds are required to prove biocompatibility. For example, poly(L-alanine-co-L-lysine) shows excellent IRI activity comparable with poly(vinyl alcohol), however, it suffers from the cytotoxicity [ 10 ]. As for biocompatible polymers, poly(ethylene glycol)s (PEGs) are the most important candidates.…”

Section: Introductionmentioning

confidence: 99%

Rediscovery of poly(ethylene glycol)s as a cryoprotectant for mesenchymal stem cells

2023

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Background A medium containing dimethyl sulfoxide (DMSO) (10% v/v) is most widely used for cell cryopreservation at –196 °C. However, residual DMSO consistently raises concerns because of its toxicity; thus, its complete removal process is required. Method As biocompatible polymers approved by the Food and Drug Administration for various biomedical applications for humans, poly(ethylene glycol)s (PEGs) with various molecular weights (400, 600, 1 K, 1.5 K, 5 K, 10 K, and 20 K Da) were studied as a cryoprotectant of mesenchymal stem cells (MSCs). Considering the cell permeability difference of PEGs depending on their molecular weight, the cells were preincubated for 0 h (no incubation), 2 h, and 4 h at 37 °C in the presence of PEGs at 10 wt.% before cryopreservation at –196 °C for 7 days. Then, cell recovery was assayed. Results We found that low molecular weight PEGs (400 and 600 Da) exhibit excellent cryoprotecting properties by 2 h preincubation, whereas intermediate molecular weight PEGs (1 K, 1.5 K, and 5 K Da) exhibit their cryoprotecting properties without preincubation. High molecular weight PEGs (10 K and 20 K Da) were ineffective as cryoprotectants for MSCs. Studies on ice recrystallization inhibition (IRI), ice nucleation inhibition (INI), membrane stabilization, and intracellular transport of PEGs suggest that low molecular weight PEGs (400 and 600 Da) exhibit excellent intracellular transport properties, and thus the internalized PEGs during preincubation contribute to the cryoprotection. Intermediate molecular weight PEGs (1 K, 1.5 K, and 5 K Da) worked by extracellular PEGs through IRI, INI, as well as partly internalized PEGs. High molecular weight PEGs (10 K and 20 K Da) killed the cells during preincubation and were ineffective as cryoprotectants. Conclusions PEGs can be used as cryoprotectants. However, the detailed procedures, including preincubation, should consider the effect of the molecular weight of PEGs. The recovered cells well proliferated and underwent osteo/chondro/adipogenic differentiation similar to the MSCs recovered from the traditional DMSO 10% system. Graphical Abstract

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Ice Recrystallization Inhibition Using l-Alanine/l-Lysine Copolymers

Cited by 8 publications

References 70 publications

High Molecular Weight Polyproline as a Potential Biosourced Ice Growth Inhibitor: Synthesis, Ice Recrystallization Inhibition, and Specific Ice Face Binding

High Molecular Weight Polyproline as a Potential Biosourced Ice Growth Inhibitor: Synthesis, Ice Recrystallization Inhibition, and Specific Ice Face Binding

Poly(l-alanine-co-l-threonine succinate) as a Biomimetic Cryoprotectant

Rediscovery of poly(ethylene glycol)s as a cryoprotectant for mesenchymal stem cells

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