Analysis of interaction between dental structural protein and adhesive component substances by circular dichroism measurement
Project/Area Number |
15390594
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
補綴理工系歯学
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Research Institution | Iwate Medical University (2005) Kyushu University (2003-2004) |
Principal Investigator |
NEZU Takashi Iwate Medical University, School of Dentistry, Lecturer, 歯学部, 講師 (40264056)
|
Co-Investigator(Kenkyū-buntansha) |
TERADA Yoshihiro Kyushu University, Faculty of Dental Science, Professor, 大学院歯学研究院, 教授 (30038898)
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Project Period (FY) |
2003 – 2005
|
Project Status |
Completed (Fiscal Year 2005)
|
Budget Amount *help |
¥13,500,000 (Direct Cost: ¥13,500,000)
Fiscal Year 2005: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2004: ¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2003: ¥8,800,000 (Direct Cost: ¥8,800,000)
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Keywords | circular dichroism / collagen / adhesive components / secondary structure / structural stability / stabilization index / hydrophobicity / 蛍光分光法 / 立体構造安定性 / 凝集性 / 接着材成分 / 誘電率 / 疎水相互作用 / 変性 |
Research Abstract |
In this project entitled "Analysis of interaction between dental structural protein and adhesive component substances by circular dichroism measurement," a circular dichroism (CD) technique was introduced to the dental research field to reveal the detailed interaction between collagen and dental-adhesive-related substances at a molecular level, and several important findings have been obtained as follows. 1. CD measurements revealed a reversible two-state structural transition of a water-soluble collagen caused by pH change of the media. At pH 3, the collagen had a conformation similar to poly(Pro)II and a DSC measurement showed a distinct endothermic peak, both indicating that the collagen was not denatured at a weakly acid pH of 3. Though an existence of hydrophobic region was expected by the formation of aggregates of the collagen at a neutral pH, no such region was proven by a fluorescence spectroscopy experiments using pyrene as a hydrophobic probe. 2. Alcoholic compounds did not af
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fect the secondary structure of the collagen, but they either lowered or raised the structural stability (denaturation temperature) of the collagen depending on their types and concentrations (and pH of the media), as observed by CD spectra and CD denaturation curves. While the great benefit of CD was shown, some limitations were also found : all materials should be soluble in appropriate solvents and the additives should be optically transparent so as not to interfere with the CD of the collagen, which are sometimes difficult in a dental adhesion research. 3. In addition to the CD experiments, a "stabilization index" of the additives has been built up by systemic DSC measurements, which is a measure of how strongly an additive stabilizes or destabilizes the collagen helix. The more hydrophobic the additive is (i.e., the smaller the specific dielectric constant is), the more effectively it lowers the structural stability of collagen. This index must valuably serve to foresee the interaction between some newly developed dental materials and dentinal collagen. Less
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Report
(4 results)
Research Products
(5 results)