| Project/Area Number |
20K20197
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| Research Category |
Grant-in-Aid for Early-Career Scientists
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| Allocation Type | Multi-year Fund |
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| Review Section |
Basic Section 90120:Biomaterials-related
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| Research Institution | Japan Advanced Institute of Science and Technology |
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Principal Investigator |
Rajan Robin 北陸先端科学技術大学院大学, 先端科学技術研究科, 助教 (70848043)
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| Project Period (FY) |
2020-04-01 – 2023-03-31
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| Project Status |
Completed (Fiscal Year 2022)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2022: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2021: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2020: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | RAFT Polymerization / Zwitterionic Polymers / Glycopolymers / Proteins / Denaturation / Ultracentrifugation / Hydrophobicity / Micelle / Protein Aggregation / Zwitterioinic polymers / hydrophobic interaction / biopharmaceutics / micelles / ultracentrifugation / Protein therapeutics / Zwitterionic Polymer / Micelles / RAFT polymerization / Protein / Zwitterionic polymer / Degradable / Glycopolymer / Polymers / Sugars / Delivery |
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| Outline of Research at the Start |
Therapeutic protein drugs are an indispensible class of pharmaceutical medicines used by patients to treat serious conditions, which cannot be otherwise treated by other drugs. Protein instability is an ongoing challenge in the field of biopharmaceutics. In this project, a novel and biodegradable micelle consisting of sugars (as core; for targeting cells), poly-SPB and a hydrophobic and a degradable moiety will be synthesized. This model can deliver the desired proteins into the cells for the treatment of numerous conditions in their native state and will be biocompatible and biodegradable.
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| Outline of Final Research Achievements |
Our research showcases successful glycopolymeric zwitterionic micelles via RAFT polymerization. These micelles effectively stabilize proteins under stress while preserving their native properties. Recovered proteins retain almost full activity. The study introduces a novel scaffold-like micellar system, enabling easily transportable protein products without low-temperature storage. Additionally, the PEG/PVA-coupled PLLSA hydrogels encapsulate proteins at therapeutic concentrations, maintaining their structure and function under extreme temperature fluctuations. The synergy between PLLSA and PEG/PVA enhances protein stabilization against freezing as well as thermal stress. These findings revolutionize long-term storage of therapeutic proteins, including antibodies and vaccines, with versatile hydrogel designs for customized protein protection and delivery under severe stress. Overall, this research advances protein-based therapeutics and preserves critical biomedical products.
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| Academic Significance and Societal Importance of the Research Achievements |
This research revolutionizes protein storage and delivery, enabling off-the-shelf products without low-temperature storage. It improves purification, processing, and production of therapeutic proteins, while offering versatile hydrogel-based protection for long-term storage.
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