Niu Lijiang, Chen Xinyong, Allen Stephanie, Tendler Saul J B
Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham NG7 2RD, U.K.
Langmuir. 2007 Jul 3;23(14):7443-6. doi: 10.1021/la7010106. Epub 2007 Jun 6.
The core recognition motif of the amyloidogenic beta-amyloid polypeptide, diphenylalanine peptide, has previously been shown to self-assemble into discrete, well-ordered, stiff nanotubes under mild conditions. The nanotubes keep the same morphology from room temperature up to 100 degrees C. In the presented study, we applied the bending beam model to atomic force microscopy images of diphenylalanine nanotubes suspended across cavities and obtained the Young's modulus 27 +/- 4 GPa and the shear modulus 0.21 +/- 0.03 GPa. We also showed that the elasticity of these nanotubes is stable within the same temperature range and at relative humidity from 0% to 70%. This study furthers our understanding of the structure and properties of these nanotubes, which are important for their potential applications in biotechnology.
淀粉样β-淀粉样多肽的核心识别基序——二苯丙氨酸肽,此前已被证明在温和条件下能自组装成离散、有序、坚硬的纳米管。这些纳米管从室温到100摄氏度都保持相同的形态。在本研究中,我们将弯曲梁模型应用于横跨空洞悬浮的二苯丙氨酸纳米管的原子力显微镜图像,得到杨氏模量为27±4吉帕,剪切模量为0.21±0.03吉帕。我们还表明,这些纳米管的弹性在相同温度范围内以及相对湿度从0%到70%时是稳定的。这项研究进一步加深了我们对这些纳米管结构和性质的理解,这对它们在生物技术中的潜在应用很重要。