4.7 Article

Oligonucleotides as Inhibitors of Ice Recrystallization

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BIOMACROMOLECULES
卷 24, 期 5, 页码 2118-2126

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AMER CHEMICAL SOC
DOI: 10.1021/acs.biomac.2c01526

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Oligonucleotides of different bases were investigated for their ice recrystallization inhibition (IRI) activity. The degree of polymerization of oligothymines was also tested. Among them, T20 showed the best IRI performance, indicating its effectiveness in preventing ice recrystallization. The IRI mechanism was further explored, and it was found that the hydrophobic interactions of T20 in the interface layer might contribute to its IRI activity.
Oligonucleotides of adenine (A20), guanine (G20), cytosine (C20), thymine (T20), cytosine-guanine ((CG)20), and adenine-thymine ((AT)20) were investigated as model compounds for ice recrystallization inhibition (IRI). Dehydroxy uracil (dU20), U20, and T20 were also compared to investigate the effect of minute changes in the hydrophobicity of the oligonucleotides on the IRI activity. Among the oligonucleotides considered in this study, T20 exhibited the best performance for IRI. In addition, the degree of polymerization of oligothymines varied over 5, 10, 20, 30, 50, and 100, and T20 was found to be the most effective for IRI. The IRI mechanism was investigated by comparing U20 and T20, which exhibited the lowest and highest IRI activity, respectively, among the oligonucleotides for their dynamic ice-shaping, thermal hysteresis, and ice nucleation inhibition. Little or no dynamic ice shaping activity and small thermal hysteresis were observed for both nucleotides. All of the findings suggest that not the ice-polymer adhesion but the hydrophobic interactions of T20 in the interface layer might interfere with the water deposition on the ice crystal surfaces and contribute to the IRI activity of the T20 oligonucleotide.

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