Advances in Atomic Force Microscopy for Probing Polymer Structure and Properties

2017 ◽  
Vol 51 (1) ◽  
pp. 3-24 ◽  
Author(s):  
Dong Wang ◽  
Thomas P. Russell
2005 ◽  
Vol 874 ◽  
Author(s):  
Stefan Habelitz ◽  
Shabnam Zartoshtimanesh ◽  
Mehdi Balooch ◽  
Sally J. Marshall ◽  
Grayson W. Marshall ◽  
...  

AbstractMice are commonly considered the model mammal for many biomedical studies. In this work, mouse and human dentin were compared to specify structural and mechanical differences to establish a baseline for comparison of dental tissues between these species. Atomic force microscopy revealed tubules of about 1.0 to 1.6 μm in diameter as the main structural feature in dentin of both species. Nanoindentation yielded the elastic modulus about 15% lower in murine intertubular dentin while the hardness was almost equal. Dynamic stiffness mapping confirmed the lower elastic properties and also revealed that the peritubular region of increased mineralization around tubules is drastically reduced or maybe absent in murine dentin of this age. This study suggests that structural and mechanical differences need to be considered when murine dentin is used as a model system.


2005 ◽  
Vol 41 (3) ◽  
pp. 277-281 ◽  
Author(s):  
Yunchang Guo ◽  
Zhongdong Liu ◽  
Hongjie An ◽  
Minqian Li ◽  
Jun Hu

1997 ◽  
Vol 77 (06) ◽  
pp. 1048-1051 ◽  
Author(s):  
Roger E Marchant ◽  
Matthew D Barb ◽  
John R Shainoff ◽  
Steven J Eppell ◽  
David L Wilson ◽  
...  

SummaryFibrinogen plays a central role in surface-induced thrombosis. However, the interactions of fibrinogen with different substrata remain poorly understood because of the difficulties involved in imaging globular proteins under aqueous conditions. We present detailed three dimensional molecular scale images of fibrinogen molecules on a hydrophobic surface under aqueous conditions obtained by atomic force microscopy. Hydrated fibrinogen monomers are visualized as overlapping ellipsoids; dimers and trimers have linear conformations predominantly, and increased affinity for the hydrophobic surface compared with monomeric fibrinogen. The results demonstrate the importance of hydration on protein structure and properties that affect surface-dependent interactions.


Sign in / Sign up

Export Citation Format

Share Document