文献类型：期刊文献

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

作者：Yu, Yuanman[1,2,3];Chen, Rui[1,2];Chen, Xinye[1,3];Wang, Jing[1,2,3];Liu, Changsheng[2,3]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, Engn Res Ctr Biomed Mat, Sch Mat Sci & Engn, Key Lab Ultrafine Mat,Minist Educ, Shanghai 200237, Peoples R China;[3]East China Univ Sci & Technol, Frontiers Sci Ctr Materiobiol & Dynam Chem, Shanghai 200237, Peoples R China

年份：2024

卷号：38

起止页码：169

外文期刊名：BIOACTIVE MATERIALS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:001230206400001)】；

基金：This research was 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) , and the China Postdoctoral Science Foundation Funded Project (2021M701192) , Fundamental Research Funds for the Central Universities (JKD01221507) , and the Foundation of Frontiers Science Center for Materiobiology and Dynamic Chemistry (JKVD1211002) .

语种：英文

外文关键词：Recombinant human bone morphogenetic; protein-2; Osteogenic activity; Protein stability; Sulfated polysaccharide

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.