Effect of DNA structure on the formation of collagen-DNA complex.
Using various types of DNAs prepared from plasmid DNA, complete double-stranded DNA (ds.DNA) with linear and cyclic forms and double-stranded DNA coexisting with single-stranded DNA (ss.DNA), the structure and fibrillogenesis of the collagen-DNA complex were investigated by means of turbidity, transmission electron microscopy, and confocal laser-scanning microscopy. The rate of fibrillogenesis of the collagen-DNA complex significantly depends on the DNA structure. The structure of the fibrils formed in the complexes showed a marked difference between the ds.DNA and ss.DNA complexes with collagen. Spatial distribution of the DNA and collagen in the complexes suggests that the characteristic collagen-DNA interaction depends on the DNA forms.
Kaya
Michiko
M
Graduate School of Environmental Earth Science, Hokkaido University, Kita-ku, Sapporo 060-0810, Japan.
Toyama
Yoshiharu
Y
Kubota
Kenji
K
Nodasaka
Yoshinobu
Y
Ochiai
Masanori
M
Nomizu
Motoyoshi
M
Nishi
Norio
N
D001672:Biocompatible Materials / Q000737:chemistry*; D003094:Collagen / Q000737:chemistry*; D004247:DNA / Q000737:chemistry*; D004277:DNA, Single-Stranded / Q000737:chemistry*; D004587:Electrophoresis, Agar Gel; D018613:Microscopy, Confocal; D046529:Microscopy, Electron, Transmission; D009391:Nephelometry and Turbidimetry; D009690:Nucleic Acid Conformation; D010434:Pepsin A / Q000737:chemistry; D010957:Plasmids / Q000378:metabolism; D011485:Protein Binding; D013997:Time Factors
D001672:Biocompatible Materials; D004277:DNA, Single-Stranded; C059821:atelocollagen; D003094:Collagen; D004247:DNA; D010434:Pepsin A