Investigations into the polymorphism of rat tail tendon fibrils using atomic force microscopy.
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 CaCl(2) could prevent this effect.
Venturoni
Manuela
M
Department of Physics, University of California, Santa Barbara, CA 93106, USA.
Gutsmann
Thomas
T
Fantner
Georg E
GE
Kindt
Johannes H
JH
Hansma
Paul K
PK
D000818:Animals; D003094:Collagen / Q000032:analysis / Q000648:ultrastructure; D020894:Microfibrils / Q000648:ultrastructure*; D018625:Microscopy, Atomic Force / Q000379:methods; D011110:Polymorphism, Genetic; D051381:Rats; D013623:Tail; D013710:Tendons / Q000648:ultrastructure*
D003094:Collagen