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Site-specific protein-protein conjugation and its application to enzymatic cascade reactions

  • 발행기관 서강대학교 일반대학원
  • 지도교수 이현수
  • 발행년도 2021
  • 학위수여년월 2021. 2
  • 학위명 석사
  • 학과 및 전공 일반대학원 화학과
  • UCI I804:11029-000000065580
  • 본문언어 영어
  • 저작권 서강대학교 논문은 저작권보호를 받습니다.

초록/요약

Research on the efficient introduction of interesting chemical groups into proteins is a very important field in chemical biology in that it reveals the structure and function of chemically modified proteins and can also produce proteins with new functions. So far, proteins can be modified using techniques such as N-terminal, C-terminal, lysine, cysteine of proteins. However, these technologies have limitations that they are difficult to introduce site specifically and low efficiency. In this study, we try to form the substrate channeling through protein-protein conjugation with a site-specific introduction using unnatural amino acid. Protein-protein conjugation has the advantages of introducing and applying certain functions that each protein has to an environment simultaneously augmented or complementary. This reaction, called Inverse Eletron Demand Diels-alder (IEDDA) reaction, can be utilized as a bio-orthogonal reaction suitable for protein-protein conjugation. Therefore, the unnatural amino acid, N6-[(1R,8S,9R)-bicyclo[6.1.0]non-4-yn-9-ylmethoxy]carbonyl-L-lysine (BCNK), and p-tetrazine-L-phenylalanine (TetF) are introduced using genetic introduction methods to different proteins and then conjugate. This connects the active site of each enzymes to form a substrate channeling, which in turn clearly improves the reaction rate of the conjugated enzyme compared to the response rate of each enzyme.

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