2004 Fiscal Year Final Research Report Summary
Studies about protein structural alteration switching using in vivo mimic system.
| Project/Area Number |
14350433
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
生物・生体工学
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| Research Institution | JAPAN ADVANCED INSTITUTE OF SCIENCE AND TECHNOLOGY |
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Principal Investigator |
TAKAGI Masahiro JAPAN ADVANCED INSTITUTE OF SCIENCE AND TECHNOLOGY, School of Material Science, Professor, 材料科学研究科, 教授 (00183434)
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| Co-Investigator(Kenkyū-buntansha) |
SHIRAKI Kentaro UNIVERSITY OF TSUKUBA, Institute of Applied Physics, Associate Professor, 物理工学系, 助教授 (90334797)
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| Project Period (FY) |
2002 – 2004
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| Keywords | Amyloid / Fibril / Aggregation / Amine / Protein |
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| Research Abstract |
Protein aggregation is facilitated by a partial unfolding during thermal or oxidative stress and byalterations in primary structure caused by mutation. Protein aggregation is a major problem in biomedical and biotechnological fields. In addition, with a growing expansion of genomic data, protein purification is one of the keys to perform post-genomic researches. In our living cells, protein aggregates are highly associated with fatal diseases, such as Alzheimer's, Creutzfeldt-Jakob, Huntington's and Parkinson's diseases. In this research, we focus on amine compounds as additive for preventing heat-induced aggregation of lysozyme, as a model protein. Furthermore, we investigated the fibrillogenesis of amyloid β and β_2-microglobulin in the presence of the additives.
We investigated whether small amine compounds prevent heat-induced aggregation and inactivation of lysozyme and fibrilization of β_2-microglobulin. The following conclusions are proposed.
(i)o-Diaminocyclohexane and p-phenylenediamine prevented heat-induced aggregation andinactivation of lysozyme. The inactivation rates of lysozyme in the presence of the additives were 3-fold slower than that in the absence of additives. (ii)p-Diaminocyclohexane and spermine prevented fibrilization of β_2-microglobulin. The rate of the fibrils in the presence of the additives is 4-fold slower than that in the absence of additives. These data provided new candidates for small additives to prevent protein aggregation.
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