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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2024.9
- 수록면
- 83 - 89 (7page)
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초록· 키워드
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Development of antibodies neutralizing SARS-CoV-2 variants is very crucial due to their therapeutic potentials and structural study on their binding mode plays an important role in the design of therapeutic antibodies. m396 is an antibody which was originally developed for SARS-CoV-1. The antibody is known to bind to the receptor binding domain (RBD) of SARSCoV-1 but not to show binding affinity against RBD of SARSCoV-2. In this study, we demonstrated that m396 scFv exhibited binding affinity to the RBD of SARS-CoV-2 Beta variant. To understand the binding mode of m396 scFv and RBD of SARSCoV-2 Beta variant, HADDOCK protein-protein docking condition was optimized and employed to model the complex structure of two proteins. Finally, the molecular interactions in the binding interface of the modeled complex were analyzed. This study suggests the possibility that m396 can be an efficient template antibody for SARS-CoV-2 variants. In addition, the optimized docking condition for the HADDOCK docking is expected to be utilized in the various computational studies on the binding of m396 and its variants against the RBDs of SARS-CoV variants.
목차
Abstract
1. INTRODUCTION
2. MATERIALS AND METHODS
3. RESULTS AND DISCUSSION
4. CONCLUSION
REFERENCES
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