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基于完好保存的结晶结构的新型丝素蛋白膜的表面分析。

Surface analysis of novel fibroin films based on well-preserved crystalline structures.

机构信息

Faculty of Fiber Science and Engineering, Kyoto Institute of Technology, Matsugasaki, Sakyo, Kyoto 606-8585, Japan.

Faculty of Fiber Science and Engineering, Kyoto Institute of Technology, Matsugasaki, Sakyo, Kyoto 606-8585, Japan.

出版信息

Int J Biol Macromol. 2021 Nov 30;191:1017-1025. doi: 10.1016/j.ijbiomac.2021.09.125. Epub 2021 Oct 1.

DOI:10.1016/j.ijbiomac.2021.09.125
PMID:34600950
Abstract

We recently reported that a highly homogeneous aqueous suspension of fibroin nanofiber (FNF) can be simply obtained by mechanical water-grinding a heterogeneous aqueous fibroin slurry and that the FNF in the suspension preserves the native β-sheet secondary structure during this mechanical treatment. The current study reports the surface properties of well-preserved crystalline structure novel FNF film from water-grinding preparation as compared with those of typical, conventionally prepared regenerated fibroin (RF) film. RF film was not treated with alcoholic solutions and was verified to be amorphous from a WAXD diffraction diagram. The air-side surfaces of the FNF semi-crystalline and RF amorphous films were studied to clarify differences using scanning electron microscopy (SEM), atomic force microscopy (AFM), attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR), static water contact angle, and X-ray photoelectron spectroscopy (XPS). The well-preserved crystalline in the FNF film was found to exist near a slightly deep surface region and to act as a physically cross-linking domain, governing the molecular motions of the amorphous polypeptide chains at the very shallow surface region.

摘要

我们最近报道称,通过机械水研磨异质丝素水浆,可以简单地获得高度均匀的丝素纳米纤维(FNF)水悬浮液,并且在该机械处理过程中,悬浮液中的 FNF 保留了天然的β-折叠二级结构。与典型的常规制备的再生丝素(RF)膜相比,本研究报告了水研磨制备的保存完好的结晶结构新型 FNF 膜的表面性能。RF 膜未经醇溶液处理,从 WAXD 衍射图中证实为非晶态。使用扫描电子显微镜(SEM)、原子力显微镜(AFM)、衰减全反射傅里叶变换红外光谱(ATR-FTIR)、静态水接触角和 X 射线光电子能谱(XPS)研究了 FNF 半结晶和 RF 非晶膜的空气侧表面,以阐明差异。在 FNF 膜中发现保存完好的结晶存在于稍深的表面区域附近,并作为物理交联域,控制非常浅的表面区域中无定形多肽链的分子运动。

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