| Co-Investigator(Kenkyū-buntansha) |
TANAKA Naoki Kyoto Institute of Technology, Faculty of Textile Science, Associate Professor, 繊維学部, 助教授 (60243127)
松本 雅光 テラメックス(株), 特機部, 課長
吉田 絵里 京都工芸繊維大学, 繊維学部, 助手 (60263175)
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| Budget Amount *help |
¥15,000,000 (Direct Cost: ¥15,000,000)
Fiscal Year 2005: ¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2004: ¥4,900,000 (Direct Cost: ¥4,900,000)
Fiscal Year 2003: ¥6,400,000 (Direct Cost: ¥6,400,000)
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| Research Abstract |
The appropriate three dimensional structures are required for the high and specific functions of proteins. However, the general mechanism of converting sequential amino acid alignments into three dimensional structures is still ambiguous. Especially, irreversible denaturation or unfolding of proteins artificially formed by way of genetic engineering methods is a big problem.
In this project, a new protein structure restoration or refolding system has been studied. There have been several attempts for protein structure restoration. They can be grouped into three categories : a-biochemical, b-chemical, and c-physicochemical. We have mainly introduced pressure as one the factor classed into c, and combined with chemical or biochemical methods.
As the first stage, some biomimetic polymers such as an elastin-model peptide, stimulus-responsive synthetic polymers, have been investigated for their pressure-temperature responsive properties (structural stability and restoration). Then, structural stability and aggregation properties of several proteins, including phosphoglycerate kinase, a double-domain protein, kumamolisin, a single-domain protein, and insulin, amyloid-forming protein, have been studied. In addition, similarity and dissimilarity of proteins and biomimetic polymers including their hydro gels have been precisely compared.
For the biochemical method, active-site fragments of molecular chaperone are targeted. Some active fragments have been prepared from cloned genes of DnaJ, ClpB and other molecular chaperones, and they were immobilized onto hydrophobic domain of phospholipid liposomes or micro-particles, to be utilized as the structure-restoration devices.
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