Effect of HEMA adsorption on the stability of native and denatured type I tendon collagen.
Adsorption behavior and stabilization/destabilization effects of 2-hydroxyethyl methacrylate (HEMA) on a bovine tendon collagen (BTC) (type I), either native (N) or thermally denatured (D), were studied by IR spectroscopy and differential scanning calorimetry (DSC). The amount of HEMA adsorbed was larger on BTC(D) than on BTC(N), because BTC(D) had a larger specific surface area (SSA) as revealed from SSA measurement. Denaturation temperature (Td) of BTC(N), measured by DSC in aqueous HEMA solution, decreased from 63 degrees C to 40 degrees C with increasing HEMA concentration (CHEMA) up to 20 wt%. This destabilization might be caused by the loss of hydrophobic stabilization of the helix structure as CHEMA was increased. At CHEMA > 20 wt%, the structure of collagen was restabilized presumably due to the dehydration effect conferred by HEMA at higher concentration. BTC(D) with little helix content, however, showed only a weak endothermic peak in the DSC measurement and the Td at 40 degrees C was independent of CHEMA.
Morikawa
Tomohiro
T
Section of Fixed Prosthodontics, Division of Oral Rehabilitation, Faculty of Dental Science, Kyushu University, 3-1-1, Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. tomohiro@dent.kyushu-u.ac.jp
Nezu
Takashi
T
Fukuda
Kyosuke
K
Terada
Yoshihiro
Y
D000327:Adsorption; D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D024042:Collagen Type I / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008689:Methacrylates / Q000737:chemistry*; D010539:Permeability; D011489:Protein Denaturation; D013055:Spectrophotometry, Infrared; D013499:Surface Properties
D024042:Collagen Type I; D008689:Methacrylates; C005044:hydroxyethyl methacrylate