1997 Fiscal Year Final Research Report Summary
Study of water structure and protein conformation in aqueous polymer solutions by Raman spectroscopy
| Project/Area Number |
08680932
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biomedical engineering/Biological material science
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| Research Institution | The university of the air |
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Principal Investigator |
HIRAKAWA Akiko The university of the air, Faculty of liberal arts, Professor, 教養学部, 教授 (00012633)
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| Co-Investigator(Kenkyū-buntansha) |
FUKUMOTO Kikuko Tokyo medical and dental university, Institute for medical and dental engineerin, 医用器材研究所, 講師
ISHIHARA Kazuhiko Tokyo medical and dental university, Institute for medical and dental engineerin, 医用器材研究所, 助教授 (90193341)
HAMADA Yoshiaki The university of the air, Faculty of liberal arts, Assistant professor, 教養学部, 助教授 (90107392)
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| Project Period (FY) |
1996 – 1997
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| Keywords | Raman spectroscopy / water soluble biomedical polymer / phospholipid polymer / denaturation of protein / structure of water |
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| Research Abstract |
Recentry, many polymeric materials have been applied in the biomedical and biological fields. It is important to consider the interaction between polymers and biological components such as proteins and cells. The water molecules are considered to exert a considerable influence on the interaction between the polymers and biological components. We studied the denaturation of proteins and change in the water structure in aqueous medium containing protein and water-soluble polymer by Raman spectroscopy. The human serum albumin (HSA) was used as protein, and poly (2-methacryloyloxyethyl phosphorylcholine) and poly (ethylene glyco1) ware used as polymers. We will make a speculation for the effect of water structure in HSA solution on the structure of HSA.And there is a close correlation between water, polymers and proteins with each other. In conclusion, the structure of the water molecules surrounding proteins affects significantly the denaturation of proteins.
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