文献类型：期刊文献

英文题名：Interaction between the Natural Lipopeptide [Glu₁, Asp₅] Surfactin-C15 and Hemoglobin in Aqueous Solution

作者：Zou, Aihua[1,2,3];Liu, Jing[1,2];Garamus, Vasil M.[1,2];Zheng, Kai[1,2];Willumeit, Regine[1,2];Mu, Bozhong[1,2]

机构：[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]E China Univ Sci & Technol, Inst Appl Chem, Shanghai 200237, Peoples R China;[3]GKSS Forschungszentrum Geesthacht GmbH, D-21502 Geesthacht, Germany

年份：2010

卷号：11

期号：3

起止页码：593

外文期刊名：BIOMACROMOLECULES

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000275164500009)】；

基金：A.Z. gratefully acknowledges the Support of this work by the Alexander von Humboldt Foundation, the support of this work by Research Fund for the New Teacher of the Doctoral Program of Higher Education of China (200802511024), the grant from the Ministry of Science and Technology of China (2007CB707801), and Shanghai Municipal Science and Technology Commission (071607014). We would like to thank Shu-Feng Sun for making FF-TEM samples in the Center for Biological Electron Microscopy, the Institute of Biophysics.

语种：英文

摘要：The interaction between natural lipopeptide [Glu(1), Asp(5)] surfactin-C15 (surfactin) and hemoglobin (Hb) has been studied. Surface tension Measurements show that the critical micelle concentration (cmc) Of surfactin increases from 1.54 x 10(-5) to 3.86 x 10(-5) mol/L with Hb. The UV spectra display that the effect Of surfactin oil Hb exhibits strong concentration-dependent fashion and the aquometHb convert to hemichrome at high surfactin concentration. Small-angle neutron scattering (SANS) and freeze-fracture transmission electron microscopy (FF-TEM) measurements show that surfactin result ill the formation of a fractal structure representing a "necklace model" of micelle-like clusters randomly distributed along the protein polypeptide chain at high surfactin concentration. Far-UV circular dichroism (CD) results confirmed that surfactin call disrupt the helical structure of protein at high concentrations, although the enhanced native-like behavior of protein by low concentration of surfactin was observed. The microenvironment change around Pile amino residues and disulfide bonds of Hb was obtained from near-UV CD spectra.