摘要
蛛丝蛋白非结晶区不同基序插入RADA16-Ⅰ,短肽分别为R1(n-RADARADAGGASRADARADA-c)和R2(n-RADARADAGPGGYRADARADA-c)。采用傅立叶红外光谱(FTIR)、原子力显微镜(AFM)和透射电子显微镜(TEM)技术研究氨基酸序列和组装时间对短肽的二级结构和自组装成的纳米结构的影响。结果表明,随着时间的延长,R1和R2形成的β-折叠片含量升高,纤维变长变宽。R1形成数量少但长达几十微米的纤维,R2形成长约一微米但数量多的纤维。通过改变氨基酸序列,控制组装时间可以达到控制自组装形成的纳米结构的目的。
Different spider fibroin non crystalline motifs GGAS and GPGGY were inserted into the middle of RADA16-Ⅰ. The resulting peptides were R1 (n-RADARADAGGASRADARADA-c) and R2 (n-RADARADAGPG- GYRADARADA-c). Fourier transform infrared spectrum (FTIR) was used to identify the secondary structure, while atomic force microscopy (AFM) and transmitting electron microscope (TEM) were used to investigate nanofibet formation of the peptides. These results illustrate that R1 and R2 form random coils and self-assemble into short fibrillar nanostruetures. R1 and R2 display a noticeable change in the formation of nanofibers with time. They become longer and wider with the increase of β-sheet content. R1 forms less and longer fibers than R2; the nanofibers formed by R2 have bend. These characteristics provide a close correlation for the roles of amino acid sequence and β-sheet structure in nanofiber formation.
出处
《生物医学工程学杂志》
EI
CAS
CSCD
北大核心
2009年第6期1276-1280,共5页
Journal of Biomedical Engineering