Interaction of collagen molecules from the aspect of fibril formation: acid-soluble, alkali-treated, and MMP1-digested fragments of type I collagen.
Collagen type I extracted with acid or digested with pepsin forms fibrils under physiological conditions, but this ability is lost when the collagen is treated with alkaline solution or digested with matrix metalloproteinase 1 (MMP1). When acid-soluble collagen was incubated with alkali-treated collagen, the fibril formation of acid-soluble collagen was inhibited. At 37 degrees C, at which alkali-treated collagen is denatured, the lag time was prolonged but the growth rate of fibrils was not affected. At 30 degrees C, at which the triple helical conformation of alkali-treated collagen is retained, the lag time was prolonged and the growth rate reduced. Heat-denatured alkali-treated collagen and MMP1-digested fragments have no inhibitory effect on the fibril formation of acid-soluble collagen. This means that the triple helical conformation and the molecular length are important factors in the interaction of collagen molecules and that alkali-treated collagen acts as a competitive inhibitor for fibril formation of collagen. We found that alkali-treated collagen and MMP1-digested fragments form fibrils that lack the D periodic banding pattern and twisted morphology under acidic conditions at the appropriate ionic strength. We also calculated the relative strengths of hydrophobic and electrostatic interactions between collagen molecules. When the hydrophobic interaction between linear collagen molecules was considered, we found a pattern of periodic maximization of the interactive force including the D period. On the other hand, the electrostatic interaction did not show the periodic pattern, but the overall interaction score affected fibril formation.
Suzuki
Y
Y
Nippi Research Institute of Biomatrix, Adachi-ku, Tokyo, 120-8601, Japan.
Someki
I
I
Adachi
E
E
Irie
S
S
Hattori
S
S
D000143:Acids / Q000737:chemistry; D000468:Alkalies / Q000494:pharmacology; D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure; D003094:Collagen / Q000737:chemistry* / Q000187:drug effects / Q000648:ultrastructure*; D003238:Connective Tissue / Q000737:chemistry / Q000187:drug effects / Q000648:ultrastructure; D006031:Glycosylation; D020781:Matrix Metalloproteinase 1 / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D011487:Protein Conformation; D011489:Protein Denaturation; D012995:Solubility; D013696:Temperature
D000143:Acids; D000468:Alkalies; D000682:Amyloid; D010446:Peptide Fragments; D003094:Collagen; D020781:Matrix Metalloproteinase 1