Interaction of giant extracellular Glossoscolex paulistus hemoglobin (HbGp) with zwitterionic surfactant N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (HPS):: Effects of oligomeric dissociation
Interaction of giant extracellular Glossoscolex paulistus hemoglobin (HbGp) with zwitterionic surfactant N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (HPS):: Effects of oligomeric dissociation
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DOI：
10.1016/j.colsurfb.2007.07.010
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发表时间：
2008-02-15
影响因子：
5.8
通讯作者：
Tabak, Marcel
中科院分区：
文献类型：
--
作者：
Moreira, Leonardo M.;Santiago, Patricia S.;Tabak, Marcel
研究了两性离子表面活性剂N-十六烷基-N，N-二甲基-3-氨基-1-丙磺酸盐(HPS)与泡状舌头虫(Glossoscolex Paulistus)巨细胞外血红蛋白(HbGp)的相互作用。利用电子光学吸收、荧光发射和圆二色谱技术，结合凝胶过滤层析，研究了HbGp与HPS的相互作用对低聚物解离和自氧化的影响。观察到HPS-HbGp相互作用的特殊行为：作为自氧化和低聚物解离过程的结果，促进了复杂的铁物种的形成平衡。在pH为7.0时，HPS在1 mM以上时效果更好，而当pH为9.0时，表面活性剂的作用在1 mM以上更为强烈。此外，HPS与HbGp的相互作用明显弱于HbGp与阳离子(CTAC)和阴离子(SDS)表面活性剂的相互作用。HPS与HPS的相互作用较弱可能是由于两个因素：(I)与HbGp与阳离子和阴离子表面活性剂之间的静电相互作用相比，HPS表面活性剂与蛋白质表面离子中心之间的静电吸引较小；(Ii)HPS的CMC较低，这可能减少了单体形式的表面活性剂与蛋白质的相互作用。本工作强调了静电作用在离子表面活性剂与HbGp相互作用中的重要性。此外，在本研究使用的整个HPS浓度范围内，未观察到该表面活性剂引起的折叠和自氧化减少。这与有关表面活性剂与四聚体血红蛋白相互作用的文献数据有很大不同，支持在低表面活性剂浓度范围内细胞内血红蛋白发生这种行为。对光谱数据进行了讨论，并与文献进行了比较，以加深对血红蛋白与表面活性剂的相互作用以及巨型胞外血红蛋白的酸性等电点(PI)对其构效关系的影响的了解。(C)2007 Elsevier B.V.保留所有权利。
The present work focuses on the interaction between the zwitterionic surfactant N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (HPS) and the giant extracellular hemoglobin of Glossoscolex paulistus (HbGp). Electronic optical absorption, fluorescence emission and circular dichroism spectroscopy techniques, together with Gel-filtration chromatography, were used in order to evaluate the oligomeric dissociation as well as the autoxidation of HbGp as a function of the interaction with HPS. A peculiar behavior was observed for the HPS-HbGp interaction: a complex ferric species formation equilibrium was promoted, as a consequence of the autoxidation and oligomeric dissociation processes. At pH 7.0, HPS is more effective up to 1 mM while at pH 9.0 the surfactant effect is more intense above 1 mM. Furthermore, the interaction of HPS with HbGp was clearly less intense than the interaction of this hemoglobin with cationic (CTAC) and anionic (SDS) surfactants. Probably, this lower interaction with HPS is due to two factors: (i) the lower electrostatic attraction between the HPS surfactant and the protein surface ionic sites when compared to the electrostatic interaction between HbGp and cationic and anionic surfactants, and (ii) the low cmc of HPS, which probably reduces the interaction of the surfactant in the monomeric form with the protein. The present work emphasizes the importance of the electrostatic contribution in the interaction between ionic surfactants and HbGp. Furthermore, in the whole HPS concentration range used in this study, no folding and autoxidation decrease induced by this surfactant were observed. This is quite different from the literature data on the interaction between surfactants and tetrameric hemoglobins, that supports the occurrence of this behavior for the intracellular hemoglobins at low surfactant concentration range. Spectroscopic data are discussed and compared with the literature in order to improve the understanding of hemoglobin-surfactant interaction as well as the acid isoelectric point (pI) influence of the giant extracellular hemoglobins on their structure-activity relationship. (c) 2007 Elsevier B.V. All rights reserved.