Hereć Monika, Islamov Akhmed, Kuklin Alexander, Gagoś Mariusz, Gruszecki Wiesław I
Department of Biophysics, Institute of Physics, Maria Curie-Skłodowska University, 20-031 Lublin, Poland.
Chem Phys Lipids. 2007 Jun;147(2):78-86. doi: 10.1016/j.chemphyslip.2007.03.007. Epub 2007 Mar 31.
Amphotericin B (AmB) is a popular antibiotic applied in treatment of deep-seated mycotic infections. The mode of action of AmB is based upon interactions with biomembranes but exact binding properties of the antibiotic to the lipid membranes still remain obscure. Effect of incorporation of AmB into egg yolk phosphatidylcholine membranes in the concentration range from 0.01 to 5 mol% on structural and dynamic properties of lipid bilayers was studied with application of small-angle neutron scattering, X-ray diffractometry and Fourier-transform infrared spectroscopy (FTIR). The results of the experiments show that AmB is located predominantly in the headgroup region of the membranes at concentrations below 1 mol%. The process of AmB aggregation, at concentrations above 1 mol%, is associated with ordering effect within the acyl chain region and therefore indicates incorporation of AmB into the hydrophobic membrane core.
两性霉素B（AmB）是一种用于治疗深部真菌感染的常用抗生素。AmB的作用方式基于其与生物膜的相互作用，但该抗生素与脂质膜的确切结合特性仍不清楚。通过小角中子散射、X射线衍射和傅里叶变换红外光谱（FTIR）研究了在0.01至5 mol%浓度范围内将AmB掺入蛋黄磷脂酰胆碱膜中对脂质双层结构和动力学性质的影响。实验结果表明，在浓度低于1 mol%时，AmB主要位于膜的头部区域。在浓度高于1 mol%时，AmB的聚集过程与酰基链区域内的有序化效应相关，因此表明AmB掺入了疏水的膜核心。
