Liquid crystalline phases of sonicated type I collagen.
The assembly properties of concentrated solutions of type I collagen molecules are compared before and after a 5-min sonication, breaking the 300-nm triple helices into short segments of about 20 nm, with a strong polydispersity. The collagen concentration of these solutions, sonicated or not, was increased up to 100 mg/ml by slow evaporation of the solvent. Whereas the non-sonicated solutions remain isotropic, the sonicated solutions transform after a few hours into a twisted liquid crystalline phase, well recognizable in polarizing microscopy. The evidence of a twisted assembly of collagen triple helices in vitro is new and relevant in a biological context since it was reported in various collagen matrices.
Giraud-Guille
M M
MM
Centre de Biologie Cellulaire CNRS, Ivry-sur-Seine, France.
D000818:Animals; D001704:Biopolymers; D002417:Cattle; D003094:Collagen / Q000648:ultrastructure; D003460:Crystallization; D008853:Microscopy / Q000379:methods; D013010:Sonication
D001704:Biopolymers; D003094:Collagen