@misc{zou_interaction_between_2010, 
author={Zou, A., Liu, J., Haramus, V.M., Zheng, K., Willumeit, R., Mu, B.},
title={Interaction between the Natural Lipopeptide [Glu1, Asp5] Surfactin-C15 and Hemoglobin in Aqueous Solution},
year={2010},
howpublished = {journal article},
doi = {https://doi.org/10.1021/bm9011453},
abstract = {The interaction between natural lipopeptide [Glu1, Asp5] 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 × 10−5 to 3.86 × 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 (FF-TEM) 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.},
note = {Online available at: \url{https://doi.org/10.1021/bm9011453} (DOI). Zou, A.; Liu, J.; Haramus, V.; Zheng, K.; Willumeit, R.; Mu, B.: Interaction between the Natural Lipopeptide [Glu1, Asp5] Surfactin-C15 and Hemoglobin in Aqueous Solution. Biomacromolecules. 2010. vol. 11, no. 3, 593-599. DOI: 10.1021/bm9011453}}