Using the bending beam model to estimate the elasticity of diphenylalanine nanotubes.
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.
Niu
Lijiang
L
Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham NG7 2RD, U.K.
Chen
Xinyong
X
Allen
Stephanie
S
Tendler
Saul J B
SJ
D004151:Dipeptides; D004548:Elasticity; D006813:Humidity; D008422:Materials Testing; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D036103:Nanotechnology; D043942:Nanotubes / Q000737:chemistry* / Q000648:ultrastructure; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry; D033081:Shear Strength; D013314:Stress, Mechanical; D013816:Thermodynamics
D004151:Dipeptides; C026650:phenylalanylphenylalanine; D010649:Phenylalanine