文献类型：期刊文献

英文题名：Interaction between the natural lipopeptide [Glu1, Asp5] surfactin-C15 and hemoglobin: A spectroscopic and electrochemical investigation

作者：Zou, Ai-hua[1]; Liu, Jing[1]; Mu, Bo-zhong[1]

机构：[1] State Key Laboratory of Bioreactor Engineering and Institute of Applied Chemistry, East China University of Science and Technology, Meilong Road 130, Shanghai 200237, China

年份：2010

卷号：369

期号：1-3

起止页码：154

外文期刊名：Colloids and Surfaces A: Physicochemical and Engineering Aspects

收录：EI(收录号：20103813252823)

语种：英文

外文关键词：Fluorescence spectroscopy - Iron compounds - Hemoglobin - Binding sites - Hydrophobicity - Fluorescence

摘要：Interactions between hemoglobin (Hb) and the natural lipopeptide [Glu1, Asp5] surfactin-C15 (surfactin) have been investigated by fluorescence spectroscopy and cyclic voltammetry. Surfactin can facilitate the conversion of aquometHb to hemichrome in 0.01M phosphate buffer solution (PBS, pH 7.4) due to the interaction between Hb and surfactin. The electrochemistry results reveal that the changes between Fe (II) and Fe (III) of heme produce a reversible process in surfactin solution as indicated by cyclic voltammograms. In other words, the electron transfer which takes place is due to the interaction between Hb and surfactin. The binding constants of surfactin on hemoglobin were calculated by the Scatchard method and the characteristic signs of the thermodynamic parameters at two classes of binding sites for surfactin on Hb were obtained. The thermodynamic function of the binding process suggests that the hydrophobic interaction is the predominant intermolecular force between Hb and surfactin. ? 2010 Elsevier B.V.