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| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Grand Ballroom |
| Time |
10월 19일 (금요일) 11:00~12:30 |
| Code |
LIFE.P-444 |
| Subject |
Enhancement antigen binding affinity of scFv-protein nanocage with SpyCatcher/SpyTag system |
| Authors |
Park Sunhee, Hyo Jin Kang1, Sang Jeon Chung2,*
Pharmacy, Sungkyunkwan University, Korea
1Department of Chemistry, Dongguk University, Korea
2College of Pharmacy, SungKyunKwan University, Korea
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| Abstract |
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 in E. coli PDHs fused to SpyTag and scFv fused to SpyCatcher. 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.
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| E-mail |
sunny21p@naver.com |
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122nd General Meeting of the KCS