Effect of HEMA Adsorption on the Stability of Native and Denatured Type I Tendon Collagen

Abstract

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（T d ）of BTC （N） , measured by DSC in aqueous HEMA solution, decreased from 63℃ to 40℃ with increasing HEMA concentration（C HEMA ）up to 20 wt％. This destabilization might be caused by the loss of hydrophobic stabilization of the helix structure as C HEMA was increased. At C HEMA ＞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 T d at 40℃ was independent of C HEMA .

Effect of pH and Addition of Salt on the Adsorption Behavior of Lysozyme on Gold, Silica, and Titania Surfaces Observed by Quartz Crystal Microbalance with Dissipation Monitoring

“…In this strategy, it is also important to have a good understanding of the adsorption phenomena on both dental materials and teeth [1][2][3] . Adsorbates may range from small organic adhesive monomers 4,5) to large polymers 6) or cells 7) , and the mechanisms underlying adsorption are diverse. Antibacterial agents may be artificial synthetic drugs or natural secreted substances.…”

New Index for the Stability of a Type I Collagen Affected by Hydrophobic Environment

“…While the content of hydroquinone in commercial products is quite small, it might be a potential substance that affects the stability of dentinal collagen even at a low concentration, deduced from the results of phenol used in this study. In the same vein, HEMA a popular dentin primer has an alcohol structure at the end of the molecule and is known to alter the stability of some collagens 5,6) . In the current study, the effect of inorganic salts was not inspected.…”

“…To date, the adsorption of a typical priming agent HEMA to a type I tendon collagen (like dentinal collagen) was proven by IR spectroscopy, and the amount of bound HEMA was directly related to the stability of collagen as determined by differential scanning calorimetry (DSC) 5) . In the same vein, it has been reported that the concentrations of HEMA and some simple alcoholic compounds affected the denaturation temperature of a tendon collagen, and likewise their alkyl chain lengths or number of hydroxyl groups 6) .…”