The effect of aluminum ions and sorbitol on collagen and skin: a thermally stimulated current spectroscopy study.
The influence of aluminum ions introduced either directly or with sorbitol, in collagen and skin, has been investigated by Thermally Stimulated Current/TSC spectroscopy. The intramolecular mobility of collagen has been found to be significantly reduced by aluminum ions. The substitution of water molecules by aluminum ions on intramolecular hydrophilic sites is suggested to be responsible for this evolution. The presence of sorbitol minimizes this effect. The intermolecular mobility of collagen is decreased upon introduction of aluminum ions in presence of sorbitol. This result can be explained by the interaction of sorbitol-aluminum entities with the telopeptidic regions of collagen molecules. In skin samples, the intra- and intermolecular mobilities are restored due to the combined actions of sorbitol and noncollagenous proteins and other macromolecules.
Gervais-Lugan
M
M
Laboratoire de Chimie de Coordination du CNRS, Toulouse, France.
Haran
R
R
Lamure
A
A
Lacabanne
C
C
D000535:Aluminum / Q000494:pharmacology*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003094:Collagen / Q000737:chemistry / Q000378:metabolism*; D003432:Cross-Linking Reagents; D008969:Molecular Sequence Data; D012867:Skin / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D013012:Sorbitol / Q000494:pharmacology*; D013053:Spectrophotometry; D013054:Spectrophotometry, Atomic
D003432:Cross-Linking Reagents; D013012:Sorbitol; D003094:Collagen; D000535:Aluminum