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Asian Journal of Biochemistry

Year: 2006 | Volume: 1 | Issue: 1 | Page No.: 18-27
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Authors

David V. Svintradze

George M. Mrevlishvili

Keywords

Research Article

Fiber Molecular Model of Collagen Triple Helix and DNA Double Helix Complex in Aqueous Solution

David V. Svintradze and George M. Mrevlishvili
The present study demonstrated the one example of biologically important and molecular self-assembly system is a collagen-DNA ordered aggregates which spontaneously forms in aqueous solution. DNA binds to collagen directly to form DNA-collagen complex. Interaction between the collagen and DNA leads to destruction of the hydration shell of the triple helix and stabilization of the double helix structure. From a molecular biology point of view this nano-scale self-assembling superstructure could increase the stability of DNA against the nucleases during collagen diseases and the growth of collagen fibrils in the presence of DNA. In addition the complex is one of the most useful carrier material for new drug and gene delivery systems as well as for gene therapy. The model suggests that DNA, containing well-arranged phosphate groups, helps the collagen to make ordered aggregates-extraordinary twisted fiber complex. The form of this complex can be controlled by variations of DNA`s molecular weight and types. This result indicates that by choosing weight and type of DNA, containing various gene vectors, can be controlled the shape of the complex. The cell recognizes the shape of DNA-collagen complex, and effectively takes up complexes of certain shapes. Therefore, it is expected that when the correlation between the shape of complex and uptake of the complex into the cell is clarified, the efficiency of introduction of DNA into cells with the use of collagen will increase even more. Such extraordinary complex induces distraction hydration shell of collagen triple helix, stabilization hydration shell of ds-DNA, stability of DNA against the nucleases and this complex between collagen and DNA determines unusual properties of collagen fibers.
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