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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-445 |
| Subject |
Clustering Effect of Interleukin-1 Receptor Antagonist on the Ferritin Nanocage |
| Authors |
Ga Hyeon Kim, Hyo Jin Kang1, Sang Jeon Chung2,*
Department of Pharmacy, Sungkyunkwan University, Korea
1Department of Chemistry, Dongguk University, Korea
2College of Pharmacy, SungKyunKwan University, Korea
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| Abstract |
Rheumatoid arthritis (RA) is a chronic, autoimmune, inflammatory systemic disease of unknown etiology characterized by persistent joint inflammation that results in progressive joint destruction, joint deformity, and physical disability.1 Interleukin-1 (IL-1) is one of the pivotal cytokines in initiating and driving the processes of RA. In the body's natural response, IL-1 receptor antagonist (IL-1Ra) has been shown conclusively to block effects of IL-1. However, in presence of the RA synovitis, the induced endogenous production of IL-1Ra is too low to contrast the high affinity of IL-1 for the cell receptors.
In this study, clustering of IL-1Ra was used to improve their therapeutic efficacy towards RA. The increased avidity of the IL-1Ra clusters may increase the biological half-life and improve the binding affinity. To this end, IL-1Ra was cloned to the N-terminus of the ferritin monomers and expressed in E. coli. Due to the local symmetry of the N-terminus of the ferritin monomers on the surface of the self-assembled nanocage, the IL-1Ras are clustered on the nanocage surface. TEM image of the purified IL-1Ra—ferritin nanoclusters revealed well-formed IL-1Ra—ferritin nanoclusters without any irregular protein aggregates. Also using surface plasmon resonance (SPR), we identified over 50-fold binding affinity of IL-1Ra clusters compared to its monomer.
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| E-mail |
rkgus1788@hanmail.net |
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122nd General Meeting of the KCS