TEMPERATURE-DEPENDENT PERTURBATION OF PHOSPHOLIPID-BILAYERS BY DIMETHYLSULFOXIDE
TEMPERATURE-DEPENDENT PERTURBATION OF PHOSPHOLIPID-BILAYERS BY DIMETHYLSULFOXIDE
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DOI：
10.1016/0005-2736(92)90139-d
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发表时间：
1992-02-17
期刊：
影响因子：
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通讯作者：
CROWE, LM
中科院分区：
文献类型：
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作者：
ANCHORDOGUY, TJ;CARPENTER, JF;CROWE, LM
二甲亚砜（DMSO）是已知的，以保护分离的酶在冷冻过程中，而在高温下不稳定的蛋白质。 这种明显的矛盾是Arakawa等人（（1990）Cryobiology 27，401-415）综述的主题，他们提出了DMSO和蛋白质的非极性部分之间的温度依赖性疏水相互作用的证据。 本研究探讨DMSO与磷脂双分子层的相互作用。 将含有羧基荧光素的磷脂囊泡在不同温度下暴露于几种浓度的DMSO。 泄漏率增加与DMSO浓度和温度。 在存在已显示可中和组织中DMSO毒性的溶质的情况下，该效应未降低。 泄漏率的增加与在较高温度下DMSO从水到辛醇的分配增加密切相关。 此外，在双层的CH 2振动的减少也被证明取决于DMSO浓度和温度。 在辛醇和DMSO的溶液中观察到CH 2振动的类似减少，表明这种效应不是通过与水的相互作用介导的。 此外，亚砜振动的研究表明，DMSO是不是氢键的辛醇的醇部分，因此，DMSO和辛醇之间的相互作用是最有可能由于疏水缔合。 这些结果与由于DMSO和双层之间的疏水缔合而在较高温度下磷脂膜的不稳定性一致。
Dimethylsulfoxide (DMSO) is known to protect isolated enzymes during freezing while destabilizing proteins at high temperatures. This apparent paradox is the subject of a review by Arakawa et al. ((1990) Cryobiology 27, 401-415), who present evidence for a temperature-dependent, hydrophobic interaction between DMSO and non-polar moieties of proteins. The present study investigates the interaction of DMSO with phospholipid bilayers. Phospholipid vesicles containing carboxyfluorescein were exposed to several concentrations of DMSO at various temperatures. Leakage rates increased with DMSO concentration and temperature. This effect was not reduced in the presence of solutes that have been shown to neutralize DMSO toxicity in tissues. The increased leakage rates correlate well with the increased partitioning of DMSO from water to octanol at higher temperatures. Additionally, reductions in the CH2 vibrations of the bilayer are also shown to depend on DMSO concentration and temperature. A similar reduction in CH2 vibrations was observed in solutions of octanol and DMSO, suggesting that this effect is not mediated through an interaction with water. Furthermore, investigation of sulfoxide vibrations indicate that DMSO is not hydrogen bonded to the alcohol moiety of octanol, and therefore the interaction between DMSO and octanol is most likely due to a hydrophobic association. These results are consistent with a destabilization of phospholipid membranes at higher temperatures due to a hydrophobic association between DMSO and the bilayer.