SMART MOLECULES: ORGANIZATION AND MORPHOLOGY OF THE SELF-ASSEMBLED COLLAGEN FIBRILS FORMED FROM A SOLUTION OF DENSLY PACKED COLLAGEN MONOMERS

摘要

Confining collagen molecules at high concentration causes them to align in the direction of molecule's long axis due to their liquid crystalline properties. Bringing the monomeric solution to the physiological condition (pH～7, 37°C temperature) initiates fibrillogencsis. Under these conditions fibrillar collagenous structures appear to condense from the monomers and retain their organization. The resulting organization of the matrix and morphology of the collagen fibrils occurs in an acellular system, in the absence of teleopeptides, and without the participation of other extracellular macromoleculcs (i.e. GAGs, PGs, etc.) thought to regulate collagen formation. This suggests that long-range structural information is encoded into the collagen triple helical domain. Considering high rate of collagen fibril production during the embryogenesis (1-3 million per hour in the chick cornea) and high concentration of collagen molecules during this period, it is difficult to believe that fibroblast cells would not take advantage of the apparent self-organizational behavior of collagen molecules during the formation of load-bearing tissue structures.Further investigations arc needed to study the effect of the other macromoleculcs on the fibril formation and possible the morphology of the fibrils (D-banding).