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Electrospinning Induced Orientation of Protein Fibrils.
Biomacromolecules ( IF 6.2 ) Pub Date : 2020-05-28 , DOI: 10.1021/acs.biomac.0c00500
Da Chen , Naagarajan Narayanan 1 , Enrico Federici , Zhi Yang 2 , Xiaobing Zuo 3 , Jinling Gao 4 , Fang Fang , Meng Deng 1 , Osvaldo H Campanella 5 , Owen G Jones
Affiliation  

Amyloid-like fibrils are prepared from protein in the lab by controlled heat treatments, yet these must be further assembled to match the desirable mechanical and structural properties of biological fibers. Here, β-lactoglobulin fibrils were incorporated into poly(ethylene oxide) fibers of 40–180 nm diameter by electrospinning. Protein fibrils presented as short segments dispersed within electrospun fibers, with no change in fibril diameter after electrospinning. Imaging analysis revealed fibrils were aligned within 20° relative to the fiber long axis, and alignment was further confirmed by polarized FTIR and anisotropic SAXS/WAXS scattering patterns. The elastic modulus of fibers increased with protein fibril content from 0.8 to 2 GPa, which is superior to reported values of silk, collagen, and gelatin. The present setup allows for manufacture of large quantities of polymeric fibers containing protein fibrils with varied diameter and mechanical strength, endowing great potential for a variety of applications.

中文翻译:

静电纺丝诱导的蛋白原纤维的取向。

淀粉样蛋白样原纤维是在实验室中通过控制热处理从蛋白质制备的,但必须进一步组装以匹配生物纤维所需的机械和结构特性。在这里,β-乳球蛋白原纤维通过电纺丝掺入直径为40-180 nm的聚环氧乙烷纤维中。蛋白质原纤维表现为分散在电纺纤维中的短节段,电纺后原纤维直径没有变化。成像分析表明,原纤维相对于纤维长轴在20°范围内排列,并通过极化FTIR和各向异性SAXS / WAXS散射图进一步证实了排列。纤维的弹性模量随蛋白质原纤维含量从0.8 GPa增至2 GPa而增加,这优于丝绸,胶原蛋白和明胶的报道值。
更新日期:2020-07-13
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