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  4. Investigations into the polymorphism of rat tail tendon fibrils using atomic force microscopy
 
research article

Investigations into the polymorphism of rat tail tendon fibrils using atomic force microscopy

Venturoni, M.
•
Gutsmann, T.
•
Fantner, G. E.  
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2003
Biochemical and Biophysical Research Communications

Collagen type I displays a typical banding periodicity of 67 nm when visualized by atomic force or transmission electron microscopy imaging. We have investigated collagen fibers extracted from rat tail tendons using atomic force microscopy, under different ionic and pH conditions. The majority of the fibers reproduce the typical wavy structure with 67 nm spacing and a height difference between the peak and the grooves of at least 5 nm. However, we were also able to individuate two other banding patterns with 23 +/- 2 nm and 210 +/- 15 nm periodicities. The small pattern showed height differences of about 2 nm, whereas the large pattern seems to be a superposition of the 67 nm periodicity showing height differences of about 20 nm. Furthermore, we could show that at pH values of 3 and below the fibril structure gets dissolved whereas high concentrations of NaCl and CaCl2 could prevent this effect. (C) 2003 Elsevier Science (USA). All rights reserved.

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Type
research article
DOI
10.1016/s0006-291x(03)00390-5
Web of Science ID

WOS:000182177800019

Author(s)
Venturoni, M.
Gutsmann, T.
Fantner, G. E.  
Kindt, J. H.
Hansma, P. K.
Date Issued

2003

Published in
Biochemical and Biophysical Research Communications
Volume

303

Issue

2

Start page

508

End page

513

Editorial or Peer reviewed

REVIEWED

Written at

OTHER

EPFL units
LBNI  
Available on Infoscience
November 5, 2010
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/56760
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