DESIGN OF ANTI-CD3 ScFv-B7.1 FUSION MOLECULE AND PREDICTION OF ITS BIOLOGICAL CHARACTERISTICS  

DESIGN OF ANTI-CD3 ScFv-B7.1 FUSION MOLECULE AND PREDICTION OF ITS BIOLOGICAL CHARACTERISTICS

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作  者:杨章民 司履生 王一理 来宝长 

机构地区:[1]Institute for Cancer Research, School of Life Science & Technology [2]Institute for Cancer Research,School of Life Science & Technology

出  处:《Academic Journal of Xi'an Jiaotong University》2002年第2期117-120,共4页西安交通大学学报(英文版)

基  金:ThisworkwassupportedbytheScientificResearchFoundationofHealthMinistryofChina(No .98 1 2 32 )

摘  要:Objective To design and construct the eukaryotic expression vector which expresses Anti-CD3 ScFv-B7.1 fusion molecules and predict the biological characteristics, the rationality and feasibility of the spacer. Methods To analyze the flexibility, Hoop & Woods hydrophilicity and the epitope of Anti-CD3 ScFv-B7.1 fusion molecule at secondary structure level by computer simulation utilizing the GoldKey software. Results By comparing with Anti-CD3 ScFv and B7.1 respectively, it shows that Anti-CD3 ScFv-B7.1 fusion molecules can form correct secondary structure with the linking of the spacer, the fusion does not change the original hydrophilicity and epitopes of both Anti-CD3 ScFv and B7.1, no new epitopes emerge; The spacer is flexible and shows low antigenicity. Conclusion The design of Anti-CD3 ScFv-B7.1 fusion molecule are rational and feasible, the expressed fusion protein could retain the maximum biological activity and the function of both Anti-CD3 ScFv and B7.1.Objective To design and construct the eukaryotic expression vector which expresses Anti-CD3 ScFv-B7.1 fusion molecules and predict the biological characteristics, the rationality and feasibility of the spacer. Methods To analyze the flexibility, Hoop & Woods hydrophilicity and the epitope of Anti-CD3 ScFv-B7.1 fusion molecule at secondary structure level by computer simulation utilizing the GoldKey software. Results By comparing with Anti-CD3 ScFv and B7.1 respectively, it shows that Anti-CD3 ScFv-B7.1 fusion molecules can form correct secondary structure with the linking of the spacer, the fusion does not change the original hydrophilicity and epitopes of both Anti-CD3 ScFv and B7.1, no new epitopes emerge; The spacer is flexible and shows low antigenicity. Conclusion The design of Anti-CD3 ScFv-B7.1 fusion molecule are rational and feasible, the expressed fusion protein could retain the maximum biological activity and the function of both Anti-CD3 ScFv and B7.1.

关 键 词:anti-CD3 SCFV B7.1 FUSION GENE COMPUTER simulation 

分 类 号:R392.11[医药卫生—免疫学]

 

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