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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >A micelle nucleation model for the interaction of dodecyl sulphate with Lys49-phospholipases A(2)
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A micelle nucleation model for the interaction of dodecyl sulphate with Lys49-phospholipases A(2)

机译：十二烷基硫酸盐与Lys49-磷脂酶A（2）相互作用的胶束成核模型

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摘要

Bothropstoxin-I (BthTx-I) is a Lys49-PLA(2) from the venom of Bothrops jararacussu that lacks detectable catalytic activity, yet causes rapid Ca2+-independent membrane damage. With the aim of understanding the interaction between BthTx-I and amphiphilic molecules, we have studied the interaction of sodium dodecyl sulphate (SDS) with the protein. Circular dichroism and attenuated total reflection Fourier-transform infrared spectra of BthTx-I reveal changes in the alpha-helical organization of the protein at an SDS/BthTx-I molar ratio of 20-25. At SDS/BthTx-I ratios of 40-45 the alpha-helices return to a native-like conformation, although fluorescence emission anisotropy measurements of 2-amino-N-hexadecyl-benzamide (AHBA) demonstrate that the total SDS is below the critical micelle concentration when this transition occurs. These results may be interpreted as the result of SDS accumulation by the BthTx-I homodimer and the formation of a pre-micelle SDS/BthTx-I complex, which may subsequently be released from the protein surface as a free micelle. Similar changes in the alpha-helical organization of BthTx-I were observed in the presence of dipalmitoylphosphatidylcholine liposomes, suggesting that protein structure transitions coupled to organization changes of bound amphiphiles may play a role in the Ca2+-independent membrane damage by Lys49-PLA(2)s. (c) 2006 Elsevier B.V. All rights reserved.
机译：Bothropstoxin-I（BthTx-1）是来自Bothrops jararacussu毒液的Lys49-PLA（2），缺乏可检测的催化活性，但会引起快速的不依赖Ca2 +的膜损伤。为了理解BthTx-1与两亲分子之间的相互作用，我们研究了十二烷基硫酸钠（SDS）与蛋白质的相互作用。 BthTx-1的圆二色性和衰减的全反射傅立叶变换红外光谱显示，当SDS / BthTx-1摩尔比为20-25时，蛋白质的α-螺旋结构发生变化。在SDS / BthTx-I比率为40-45的情况下，尽管对2-氨基-N-十六烷基-苯甲酰胺（AHBA）的荧光发射各向异性进行了测量，结果表明，总SDS低于临界值，但α-螺旋却恢复了类似天然的构象。发生这种转变时的胶束浓度。这些结果可以解释为由BthTx-1同型二聚体引起的SDS积累和胶束前SDS / BthTx-1复合物的形成的结果，其随后可以作为游离胶束从蛋白质表面释放。在存在二棕榈酰磷脂酰胆碱脂质体的情况下，观察到了BthTx-1的α螺旋结构的类似变化，这表明蛋白质结构转变与结合的两亲物的组织变化偶联可能在Lys49-PLA引起的Ca2 +非依赖性膜破坏中起作用）s。 （c）2006 Elsevier B.V.保留所有权利。

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