Regulating the bioactivity of non-glycosylated recombinant human bone morphogenetic protein-2 to enhance bone regeneration  

作　　者：Yuanman Yu Rui Chen Xinye Chen Jing Wang Changsheng Liu 

机构地区：[1]The State Key Laboratory of Bioreactor Engineering,East China University of Science and Technology,Shanghai,200237,PR China [2]Key Laboratory for Ultrafine Materials of Ministry of Education,Engineering Research Center for Biomedical Materials of Ministry of Education,School of Materials Science and Engineering,East China University of Science and Technology,Shanghai,200237,PR China [3]Frontiers Science Center for Materiobiology and Dynamic Chemistry,East China University of Science and Technology,Shanghai,200237,PR China

出　　处：《Bioactive Materials》2024年第8期169-180,共12页生物活性材料（英文）

基　　金：supported by the Basic Science Center Program of National Natural Science Foundation of China(No.T2288102);the Key Program of the National Natural Science Foundation of China(No.32230059);the National Natural Science Foundation of China(No.32101086);the National Postdoctoral Program for Innovative Talents(BX2021101);the China Postdoctoral Science Foundation Funded Project(2021M701192);Fundamental Research Funds for the Central Universities(JKD01221507);the Foundation of Frontiers Science Center for Materiobiology and Dynamic Chemistry(JKVD1211002).

摘　　要：Recombinant human bone morphogenetic protein-2(rhBMP-2)is the predominant growth factor that effectively induces osteogenic differentiation in orthopedic procedures.However,the bioactivity and stability of rhBMP-2 are intrinsically associated with its sequence,structure,and storage conditions.In this study,we successfully determined the amino acid sequence and protein secondary structure model of non-glycosylated rhBMP-2 expressed by an E.coli expression system through X-ray crystal structure analysis.Furthermore,we observed that acidic storage conditions enhanced the proliferative and osteoinductive activity of rhBMP-2.Although the osteogenic activity of non-glycosylated rhBMP-2 is relatively weaker compared to glycosylated rhBMP-2;however,this discrepancy can be mitigated by incorporating exogenous chaperone molecules.Overall,such information is crucial for rationalizing the design of stabilization methods and enhancing the bioactivity of rhBMP-2,which may also be applicable to other growth factors.

关 键 词：Recombinant human bone morphogenetic protein-2 Osteogenic activity Protein stability Sulfated polysaccharide 

分 类 号：R318[医药卫生—生物医学工程]