Liquid crystalline phases of sonicated type I collagen
- 1 January 1989
- journal article
- research article
- Published by Wiley in Biology of the Cell
- Vol. 67 (1), 97-101
- https://doi.org/10.1111/j.1768-322x.1989.tb03014.x
Abstract
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 increase 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.Keywords
This publication has 6 references indexed in Scilit:
- Spatial organization of collagen in annelid cuticle: order and defectsBiology of the Cell, 1988
- Twisted architectures in cell‐free assembled collagen gels: study of collagen substrates used for culturesBiology of the Cell, 1985
- Extracellular compartments in matrix morphogenesis: collagen fibril, bundle, and lamellar formation by corneal fibroblasts.The Journal of cell biology, 1984
- Rotary shadowing of extended molecules dried from glycerolJournal of Ultrastructure Research, 1980
- Quasi-hexagonal molecular packing in collagen fibrilsNature, 1979
- The formation of fibrils from collagen solutions 1. The effect of experimental conditions: kinetic and electron-microscope studiesBiochemical Journal, 1960