2023 Fiscal Year Final Research Report
ring the potential for amino acid polymerization and asymmetric amplification inside ice planets
| Project/Area Number |
21K18643
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| Research Category |
Grant-in-Aid for Challenging Research (Exploratory)
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| Allocation Type | Multi-year Fund |
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| Review Section |
Medium-sized Section 17:Earth and planetary science and related fields
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| Research Institution | The University of Tokyo |
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Principal Investigator |
KAGI HIROYUKI 東京大学, 大学院理学系研究科(理学部), 教授 (70233666)
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| Co-Investigator(Kenkyū-buntansha) |
三村 耕一 名古屋大学, 環境学研究科, 教授 (80262848)
奈良 雅之 東京医科歯科大学, 教養部, 教授 (90301168)
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| Project Period (FY) |
2021-07-09 – 2024-03-31
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| Keywords | アミノ酸 / 高圧 |
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| Outline of Final Research Achievements |
Amino acids are the basic building blocks of proteins. We have found that amino acids dehydrate and condense under high pressure at room temperature to form long-chain peptides. Under relatively low temperature conditions near room temperature, polymerisation reactions are expected to occur with preserved optical activity, as racemisation does not proceed. Noting that the amino acids in the meteorite have an excess of L-body, the possibility of asymmetric enrichment of the L-body during apolymerisation under high pressure was investigated. In this study, the sequence of optical isomers constituting the dimer and trimer of amino acids was rigorously determined and a method was developed to quantitatively assess asymmetric enrichment.
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| Free Research Field |
地球内部化学
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| Academic Significance and Societal Importance of the Research Achievements |
ホモキラリティの起源を知る目的で、高圧下でのアミノ酸の重合過程における不斉濃縮の可能性を検討した。ペプチド（ただし3量体まで）のアミノ酸の配列を光学異性体を含めて解析する手法を確立することができた。これまでの結果では、アミノ酸の重合過程で有意に多く生成する三量体も見られており、何らかの不斉濃縮が起こった可能性は残されている。
高圧下での重合反応は環境に負荷がかかる触媒を必要とせず、室温で進行するため光学異性体が保存されるため、医薬品の合成などに応用が可能かも知れない。
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