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- W2012201478 abstract "Surface pressure-molecular area (Π-A) isotherms and fluorescence microscopy were used to investigate the interactions between N-stearoyl-glutamic acid (l- and d-) and l-arginine at the air/water interface. N-stearoyl-glutamic acids (C18-Glu) with different chirality (l- and d-) were spread at the air–water interface onto subphases containing varied concentrations of l-arginine at pH 5. The apparent binding affinity of C18-Glu to l-arginine was obtained by fitting the plots of the change in mean molecular area of C18-Glu vs. l-arginine concentration. The thermodynamic properties of the binding events such as binding constant and Gibbs free energy were estimated from the binding curves. We found that N-stearoyl-l-glutamic acid (C18-l-Glu) had a stronger binding affinity to l-arginine as compared to N-stearoyl-d-glutamic acid (C18-d-Glu) at low to moderate surface pressures (below ∼22 mN/m). The C18-d-Glu had stronger binding to l-arginine at higher surface pressure. Domains with different shapes in C18-l-Glu and C18-d-Glu monolayers were observed under a fluorescence microscope in situ at the air/water interface. Herein, we present a mechanism for C18-l-Glu and C18-d-Glu interacting with l-arginine at the air/water interface." @default.
- W2012201478 created "2016-06-24" @default.
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- W2012201478 date "2013-10-01" @default.
- W2012201478 modified "2023-10-16" @default.
- W2012201478 title "Thermodynamic analysis and fluorescence imaging of homochiral amino acid–amino acid interactions at the air/water interface" @default.
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- W2012201478 doi "https://doi.org/10.1016/j.jcis.2013.07.020" @default.
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