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Investigation of dynamic behaviors and morphology change of anionic phospholipid DPPG monolayer caused by BSA at air-water interface
hao
作者单位E-mail
hao 陕西师范大学 haochangchun@snnu.edu.cn 
摘要:
In this article, the interaction between bovine serum albumin (BSA) and the anionic 1.2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt) (DPPG) phospholipid was investigated at air-water interface through surface pressure measurements and atomic force microscopy (AFM) observation. By analyzing surface pressure-mean molecular area (π - A) isotherms, the limiting molecular area in the closed packing state-the concentration of BSA (Alim-[BSA]) isotherms, the compressibility coefficient-surface pressure ( -π) curves and the difference value of mean molecular area-the concentration of BSA (?A-[BSA]) isotherms, the results indicated that the mean molecular area of DPPG monolayer became much larger at pH=3 and 5 when the concentration of BSA in the subphase increased, but the isotherms kept the same shape at different amount of BSA at pH=10. Certain amount of BSA molecules could insert into the lipid monolayer to reach a saturated state. From the surface pressure-time (π - t) data, we obtain that BSA molecules were absorbed into DPPG monolayer for pH=3 and 5, and the occurrence of desorption process was observed for pH=10. The reason is that the interaction between BSA and DPPG is mainly the electrostatic interaction. AFM images revealed that the subphase pH and the concentration of BSA could affect the morphology features of the monolayers. The observed results were consistent with the curves. The study is provides an important experimental basis and theoretical support to understand the interaction between lipid and BSA in the air-liquid interface.
关键词:  bovine serum albumin  DPPG  isotherm  interaction
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Investigation of dynamic behaviors and morphology change of anionic phospholipid DPPG monolayer caused by BSA at air-water interface
changchun
Abstract:
In this article, the interaction between bovine serum albumin (BSA) and the anionic 1.2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt) (DPPG) phospholipid was investigated at air-water interface through surface pressure measurements and atomic force microscopy (AFM) observation. By analyzing surface pressure-mean molecular area (π - A) isotherms, the limiting molecular area in the closed packing state-the concentration of BSA (Alim-[BSA]) isotherms, the compressibility coefficient-surface pressure ( -π) curves and the difference value of mean molecular area-the concentration of BSA (?A-[BSA]) isotherms, the results indicated that the mean molecular area of DPPG monolayer became much larger at pH=3 and 5 when the concentration of BSA in the subphase increased, but the isotherms kept the same shape at different amount of BSA at pH=10. Certain amount of BSA molecules could insert into the lipid monolayer to reach a saturated state. From the surface pressure-time (π - t) data, we obtain that BSA molecules were absorbed into DPPG monolayer for pH=3 and 5, and the occurrence of desorption process was observed for pH=10. The reason is that the interaction between BSA and DPPG is mainly the electrostatic interaction. AFM images revealed that the subphase pH and the concentration of BSA could affect the morphology features of the monolayers. The observed results were consistent with the curves. The study is provides an important experimental basis and theoretical support to understand the interaction between lipid and BSA in the air-liquid interface.
Key words:  bovine serum albumin  DPPG  isotherm  interaction