中国物理B ›› 2016, Vol. 25 ›› Issue (9): 90506-090506.doi: 10.1088/1674-1056/25/9/090506
• SPECIAL TOPIC—Physical research in liquid crystal • 上一篇 下一篇
Xiaolong Lu(逯晓龙), Ruixin Shi(史瑞新), Changchun Hao(郝长春), Huan Chen(陈欢), Lei Zhang(张蕾), Junhua Li(李俊花), Guoqing Xu(徐国庆), Runguang Sun(孙润广)
Xiaolong Lu(逯晓龙)1, Ruixin Shi(史瑞新)2, Changchun Hao(郝长春)1, Huan Chen(陈欢)1, Lei Zhang(张蕾)1, Junhua Li(李俊花)1, Guoqing Xu(徐国庆)1, Runguang Sun(孙润广)1
摘要: The interaction between proteins and lipids is one of the basic problems of modern biochemistry and biophysics. The purpose of this study is to compare the penetration degree of lysozyme into 1,2-diapalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phosphoethano-lamine (DPPE) by analyzing the data of surface pressure-area (π-A) isotherms and surface pressure-time (π-T) curves. Lysozyme can penetrate into both DPPC and DPPE monolayers because of the increase of surface pressure at an initial pressure of 15 mN/m. However, the changes of DPPE are larger than DPPC, indicating stronger interaction of lysozyme with DPPE than DPPC. The reason may be due to the different head groups and phase state of DPPC and DPPE monolayers at the surface pressure of 15 mN/m. Atomic force microscopy reveals that lysozyme was absorbed by DPPC and DPPE monolayers, which leads to self-aggregation and self-assembly, forming irregular multimers and conical multimeric. Through analysis, we think that the process of polymer formation is similar to the aggregation mechanism of amyloid fibers.
中图分类号: (Thermodynamics)