MORPHOLOGY OF ADSORBED COLLAGEN LAYERS OBSERVED BY ATOMIC FORCE MICROSCOPY

2009 ◽  
Vol 21 (05) ◽  
pp. 311-316
Author(s):  
Yih-Pey Yang ◽  
Chia-Chi Lin

The interaction between cells and biomaterials strongly depends on the assembled structure of collagen adsorption upon the solid surface. Due to its self-assembling property, Type I collagen may aggregate and form fibrils in vivo and in vitro. This study utilizes an atomic force microscope to investigate nanometer-scale organization of adsorbed Type I collagen layers on mica and on poly(methyl methacrylate) (PMMA). We have observed various film morphologies, depending on substrate hydrophobicity and the state of collagen solution used. On mica, the atomic force microscopy (AFM) study obtains dense felt-like structures of randomly distributed assemblies. Images of network-like assemblies composed of interwoven fibrils appear on PMMA. According to the above results, we believe that these assemblies are associated at the interface rather than aggregated in the solution. This work also investigates the adsorbed collagen structure on PMMA after collagen aggregation in solution, to realize the relation between adsorption and aggregation. Consequently, the result exhibits a dendritic fibrillar structure adsorbed on PMMA, following collagen molecule aggregation, to form a fibrillar structure in the solution. This result suggests that the adsorption of aggregates preformed in the solution is preferable to collagen molecules adsorption. This research created all assembled structures of adsorbed collagen layers in nanometer-scale thickness.

2010 ◽  
Vol 98 (3) ◽  
pp. 29a
Author(s):  
Arkady Bitler ◽  
Emanuel Perugia ◽  
Inna Solomonov ◽  
Robert Visse ◽  
Joseph Orgel ◽  
...  

2017 ◽  
Vol 2017 ◽  
pp. 1-14 ◽  
Author(s):  
Andreas Stylianou

Novel nanobiomaterials are increasingly gaining ground in bioengineering research. Among the numerous biomaterials, collagen-nanobiomaterials, such as collagen thin films, are of great interest since they present a wide range of applications in the fields of biomaterials, tissue engineering, and biomedicine. Collagen type I is the most abundant protein within extracellular matrix and, due to its unique characteristics, is widely used as biomaterial. A thorough characterization of the structure and properties of nanomaterials can be achieved by Atomic Force Microscopy (AFM). AFM is a very powerful tool which can be used to obtain qualitative or quantitative information without destroying the collagen fibrillar structure. This mini review covers issues related to the use of AFM for studying the structure and mechanical properties of collagen-based nanobiomaterials, collagen-substrate interactions during the formation of collagen thin films, collagen-cells interactions, and the collagen-optical radiation interactions.


2010 ◽  
Vol 107 (38) ◽  
pp. 16530-16535 ◽  
Author(s):  
J. Liu ◽  
G. E. R. Weller ◽  
B. Zern ◽  
P. S. Ayyaswamy ◽  
D. M. Eckmann ◽  
...  

The Analyst ◽  
2019 ◽  
Vol 144 (16) ◽  
pp. 4985-4994
Author(s):  
Alison O. Nwokeoji ◽  
Sandip Kumar ◽  
Peter M. Kilby ◽  
David E. Portwood ◽  
Jamie K. Hobbs ◽  
...  

Atomic force microscopy (AFM) in conjunction with ion-pair reverse-phase high performance liquid chromatography (IP-RP-HPLC) provides novel insight into dsRNA for RNAi applications.


The Analyst ◽  
2019 ◽  
Vol 144 (22) ◽  
pp. 6773-6773
Author(s):  
Alison O. Nwokeoji ◽  
Sandip Kumar ◽  
Peter M. Kilby ◽  
David E. Portwood ◽  
Jamie K. Hobbs ◽  
...  

Correction for ‘Analysis of long dsRNA produced in vitro and in vivo using atomic force microscopy in conjunction with ion-pair reverse-phase HPLC’ by Alison O. Nwokeoji, et al., Analyst, 2019, 144, 4985–4994.


Sign in / Sign up

Export Citation Format

Share Document