Insights into the mechanism of how Morin suppresses amyloid fibrillation of hen egg white lysozyme

Publication date: August 2017
Source:International Journal of Biological Macromolecules, Volume 101
Author(s): Xiaoying Chong, Luchen Sun, Yonghui Sun, Lin Chang, Alan K. Chang, Xian Lu, Xuejie Zhou, Junqing Liu, Bing Zhang, Gary W. Jones, Jianwei He
This communication describes the inhibitory effect of Morin on the fibrillation of Hen Egg White Lysozyme (HEWL), a generic amyloid-forming model protein. This effect was dose-dependent and stronger than other small molecules we have tested previously. Spectrofluorometric and computational studies support a model suggesting that Morin inhibits amyloid fibril formation of HEWL by binding to the aggregation prone cleft region of the β-domain of HEWL, thereby stabilizing the molecule in its native-like state. Interestingly, transmission electron microscopy observations suggest that, along with increases in Morin concentration, the observed amorphous aggregates became larger and morphologically different. We propose that following occupation of the binding cleft, excess Morin adheres and coats the HEWL protein surface, thereby minimizing the interaction between the protein surface and water molecules.



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