New index for the stability of a type I collagen affected by hydrophobic environment.
Effects of hydrophobic environment adjusted by various alcohols on the structural stability of calfskin collagen (CSC) were studied to elucidate the nature of collagen-monomer interaction in adhesion. The stability of CSC in aqueous alcohol solutions was represented by its denaturation temperature, Td, measured by DSC. The hydrophobicity of the alcohol solutions was quantified with their specific dielectric constants, epsilon(r), calculated from their concentrations. The effect of each alcohol to stabilize or destabilize CSC was evaluated by the initial slope of each Td vs. epsilon(r) plot, denoted as -(dTd/d epsilon(r))ini and termed as stabilization power. Results showed that a hydrophobic environment with a smaller epsilon(r) lowered the stabilization power. Stabilization power ranged from -3 (strong destabilization) for phenol (epsilon(r) =12) to +0.3 (weak stabilization) for glycerol (epsilon(r)=47). In view of the encouraging results obtained in this study, the new index was therefore helpful in predicting the effects of new dental materials of known epsilon(r) values on the stability of dentinal collagen.
Nezu
Takashi
T
Dental Biomaterials and Technology, Iwate Medical University School of Dentistry, 1-3-27 Chuo-dori, Morioka 020-8505, Japan. tnezu@iwate-med.ac.jp
Morikawa
Tomohiro
T
Sasaki
Kaori
K
Saitoh
Setsuo
S
Taira
Masayuki
M
Terada
Yoshihiro
Y
Araki
Yoshima
Y
D000438:Alcohols / Q000494:pharmacology*; D000818:Animals; D002417:Cattle; D024042:Collagen Type I / Q000737:chemistry* / Q000187:drug effects; D006863:Hydrogen-Ion Concentration / Q000187:drug effects; D057927:Hydrophobic and Hydrophilic Interactions
D000438:Alcohols; D024042:Collagen Type I