Silk Fibroin Self-Assembly at the Air–Water Interface

O. Milyaeva, A. Akentiev, A. Bykov, Reinhard Miller, A. R. Rafikova, Kseniya Yu. Rotanova, B. Noskov
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Abstract

Amphiphilic silk fibroin (SF) forms stable adsorption layers at the air–water interface. The range of the investigated protein concentrations can be divided into two parts according to the peculiarities of the surface layer properties. At protein concentrations from 0.0005 to 0.01 mg/mL, the dynamic surface elasticity monotonically increases with the concentration and surface age and reaches values of up to 220 mN/m. In this range, the adsorption layer compression leads to a fast increase of the surface pressure. In the second part (>0.01 mg/mL), the surface elasticity decreases again and the kinetic dependences of the film thickness and adsorbed amount change only a little. In this case, the layer compression leads only to a slight increase of the surface pressure. These two types of behavior can be attributed to the distinctions in the protein aggregation in the surface layer. Atomic force microscopy (AFM) investigations of the layers transferred from the liquid surface onto a mica surface by the Langmuir–Schaefer method show some peculiarities of the layer morphology in the intermediate concentration range (~0.02 mg/mL).
空气-水界面上的蚕丝纤维素自组装
两性蚕丝纤维素(SF)在空气-水界面形成稳定的吸附层。根据表层特性的特殊性,所研究的蛋白质浓度范围可分为两部分。当蛋白质浓度为 0.0005 至 0.01 mg/mL 时,动态表面弹性随浓度和表面龄期的增加而单调增加,最高可达 220 mN/m。在此范围内,吸附层压缩导致表面压力快速增加。在第二部分(>0.01 毫克/毫升),表面弹性再次降低,薄膜厚度和吸附量的动力学依赖关系变化很小。在这种情况下,膜层压缩只会导致表面压力的轻微增加。这两种行为可归因于表层蛋白质聚集的不同。用 Langmuir-Schaefer 方法对从液体表面转移到云母表面的表层进行的原子力显微镜(AFM)研究表明,在中间浓度范围(约 0.02 毫克/毫升)内,表层形态有一些特殊性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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