文献类型：期刊文献

英文题名：Interaction between the natural lipopeptide [Glu1, Asp 5] surfactin-C15 and hemoglobin in aqueous solution

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

机构：[1] State Key Laboratory of Bioreactor Engineering and Institute of Applied Chemistry, East China University of Science and Technology, Shanghai 200237, China; [2] GKSS Research Center, Max-Planck-Str. 1, 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：EI(收录号：20101312812527)

语种：英文

外文关键词：Covalent bonds - Sulfur compounds - Neutron scattering - Critical micelle concentration - Dichroism - High resolution transmission electron microscopy - Micelles - Circular dichroism spectroscopy - Solutions

摘要：The interaction between natural lipopeptide [Glui, Asps] 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 10-5to 3.86 x 10-5 mol/L with Hb. The UV spectra display that the effect of surfactin on 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 (FFTEM) measurements show that surfactin result in 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 can 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 Phe amino residues and disulfide bonds of Hb was obtained from near-UV CD spectra. ? 2010 American Chemical Society.