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  • 02월 28일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제123회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Enhancement antigen binding affinity of scFv-protein nanocage with SpyCatcher/SpyTag system

2019년 2월 13일 09시 46분 55초
LIFE.P-363 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
4월 19일 (금요일) 11:00~12:30
Life Chemistry
저자 및
Park Sunhee, Sang Jeon Chung1,*
Pharmacy, Sungkyunkwan University, Korea
1College of Pharmacy, SungKyunKwan University, Korea
Single chain variable fragments (scFvs) have potential advantages over whole antibodies, scFvs are one-fifth the size of whole antibodies, they retain antigen binding capacity. It is smaller than IgG but it can binding with antigen and easily make with E.coli system. But scFv ‘s half-life is shorter than intact, Fc-containing IgG molecule. For exceeding the limit, we use pyruvate dehydrogenase multienzyme complex (PDH). The PDH can self-assembled highly symmetric structure. PDH is composed of 60 subunits, which are self-assembled to form a cage-like nanostructure with external diameter of 23.7 nm[1]. Here we establish a platform for irreversibly conjugating PDHs simply by mixing with protein scFv. We expressed PDHs fused to SpyTag and scFv fused to SpyCatcher in E. coli. SpyCatcher is a genetically-encoded protein designed to spontaneously form a covalent bond to its peptide-partner SpyTag[2]. Using this SpyTag/Catcher system, scFvs have potential advantages over whole antibodies. In this study, we developed the therapeutic potential and safety profiles of high affinity protein nanocage (scFv-PDH) targeted HER2 antigen which are identified using a scFv variant of Trastuzumab and modified PDH. We show that protein nanocage demonstrate high binding affinity and specificity to HER2 antigen.