کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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5367852 | 1388374 | 2011 | 7 صفحه PDF | دانلود رایگان |

The effect of tryptophan on the membrane stability was studied by using three artificial biological membranes including liposome, Langmuir monolayer and solid supported bilayer lipid membrane (s-BLM) as models. All the results indicate that the penetration of tryptophan can destabilize different artificial biological membranes. The diameter of liposome and the leakage of calcein from liposome increased with the increase of tryptophan concentration because the penetration of tryptophan was beneficial for dehydrating the polar head groups of lipids and the formation of fusion intermediates. Ï-A isotherms of lecithin on the subphase of tryptophan solution further confirm that tryptophan can penetrate into lipid monolayer and reduce the stability of lipid monolayer. When the concentration of tryptophan increased from 0 to 2 Ã 10â3 mol Lâ1, the limiting molecular area of lecithin increased from 110.5 to 138.5 à 2, but the collapse pressure of the monolayer decreased from 47.6 to 42.3 mN mâ1, indicating the destabilization of lipid monolayer caused by the penetration of tryptophan. The resistance spectra of s-BLM demonstrate that the existence of tryptophan leads to the formation of some defects in s-BLM and the destabilization of s-BLM. The values of electron-transfer resistance and double layer capacitance respectively decreased from 5.765 Ã 106 Ω and 3.573 Ã 10â8 F to 1.391 Ã 106 Ω and 3.340 Ã 10â8 F when the concentration of tryptophan increased from 0 to 2 Ã 10â3 mol Lâ1. Correspondingly, the breakdown voltage of s-BLM decreased from 2.51 to 1.72 V.
Research highlightsâ¶ The penetration of tryptophan can destabilize artificial biological membranes. â¶ The penetration of tryptophan is beneficial for liposome fusion. â¶ Tryptophan can penetrate into lipid monolayer and reduce its stability. â¶ The existence of tryptophan leads to the formation of some defects in s-BLM.
Journal: Applied Surface Science - Volume 257, Issue 11, 15 March 2011, Pages 5070-5076