Arginine induces protein self-assembly into nanofibers for triggering osteogenic differentiation of stem cells
Arginine induces protein self-assembly into nanofibers for triggering osteogenic differentiation of stem cells
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精氨酸诱导蛋白质自组装成纳米纤维,从而触发干细胞的成骨分化
DOI:
10.1039/d1tb01921j
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发表时间:
2021
影响因子:
7
通讯作者:
Yang Mingying
中科院分区:
文献类型:
--
作者:
Lei Fang;Zhou Guanshan;Chen Yuping;Cai Jiangfeng;Wang Jie;Shuai Yajun;Xu Zongpu;Wang Zhangfu;Mao Chuanbin;Yang Mingying
Although silk proteins are considered promising in building a scaffold for tissue engineering, one of the silk proteins, Bombyx mori silk sericin (BS), has limited processability in producing nanofibrous scaffolds because its surface charge anisotropy promotes gelation instead. To overcome this daunting challenge, we developed a mild and simple procedure for assembling BS into nanofibers and nanofibrous scaffolds. Briefly, arginine was added to the aqueous BS solution to reduce the negative charge of BS, thereby inducing BS to self-assemble into nanofibers in the solution. Circular dichroism (CD) and Fourier transform infrared (FT-IR) spectra showed that arginine promoted the formation of β-sheet conformation in BS and increased its thermal stability. Furthermore, the arginine-induced BS nanofiber solution could be casted into scaffolds made of abundant network-like nanofibrous structures. The BS scaffolds promoted cell adhesion and growth and stimulated osteogenic differentiation of the bone marrow mesenchymal stem cells (BMSCs) in the absence of differentiation inducers in culture media. Our study presents a new strategy for assembling proteins into osteogenic nanofibrous scaffolds for inducing stem cell differentiation in regenerative medicine.