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2021 Fiscal Year Final Research Report

Elucidation of LEA peptides function in enhancing of protein expression

Research Project

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Project/Area Number 19K05168
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeMulti-year Fund
Section一般
Review Section Basic Section 27040:Biofunction and bioprocess engineering-related
Research InstitutionKyushu Institute of Technology

Principal Investigator

Ikeno Shinya  九州工業大学, 大学院生命体工学研究科, 准教授 (20437792)

Project Period (FY) 2019-04-01 – 2022-03-31
Keywords組換えタンパク質発現 / 大腸菌 / LEAペプチド / シャペロン様活性 / 分子シールド機能 / 分子クラウディング / LEAタンパク質 / GFP
Outline of Final Research Achievements

We hypothesized a "molecular shield function" to suppress protein-protein aggregation and a "molecular chaperone-like function" to promote protein folding in order to elucidate the function of LEA peptides, which increase the expression of recombinant proteins in E. coli. The results of the molecular shield function elucidation using synthetic LEA peptides showed that LEA peptides did not suppress protein aggregation induced by heat or salt. On the other hand, the expression levels of target proteins were evaluated by the addition of synthetic LEA peptides using a cell-free protein synthesis system, and the expression levels of target proteins were significantly increased. These results suggest that LEA peptides may have a molecular chaperone-like function in cells.

Free Research Field

生物機能工学

Academic Significance and Societal Importance of the Research Achievements

本研究で開発したLEAペプチド共発現法は、特徴としてペプチド遺伝子を細胞に導入するのみで組換えタンパク質の発現増大し、他の宿主への適用が容易な点にある。そして発現したペプチドは非常に小分子であるため、その除去精製プロセスは非常に簡便である。本研究で取り組んだLEAペプチドの作用機序の解明により、ペプチドにより引き起こされる生体内の現象が明らかになり、それらを調節・制御する新しい方法論の確立につながるため学術的意義も非常に高い。

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Published: 2023-01-30  

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