Recombinant expression and characterization of an epididymis-specific antimicrobial peptide BIN1b/SPAG11E
文献类型：期刊论文
| 作者 | Guo, Chenyun2; Diao, Hua1,3; Lian, Yandong2; Yu, Heguo1; Gao, Hongchang2; Zhang, Yonglian1,3; Lin, Donghai2 |
| 刊名 | JOURNAL OF BIOTECHNOLOGY
 |
| 出版日期 | 2009 |
| 卷号 | 139期号:1页码:33-37 |
| 关键词 | BIN1b Size-exclusion CD HSQC Oligomerization Antimicrobial activity |
| ISSN号 | 0168-1656 |
| DOI | 10.1016/j.jbiotec.2008.10.003 |
| 文献子类 | Article |
| 英文摘要 | BIN1b was reported as all epididymis-specific beta-defensin antimicrobial peptide. In this paper. the recombinant BIN1b was expressed and purified by fusing with GB1-His tag. The size-exclusion gel filtration experiment indicated that the fusion protein GB1-BIN1b formed multimers at pH 7.4. and existed as monomer at pH 4.5. The oligomerization of GB1-BIN1b was only related to PH value, neither to NaCl concentration nor protein concentration. Far-UV circular dichroism (CD) spectra also showed the fusion protein had more ordered secondary structures at pH 4.5 than at pH 7.4,as a negative peak appeared around 218 nm indicative of typical beta-sheet. The 2D N-15-H-1 heteronuclear single-quantum coherence (HSQC) spectra suggested that the fusion protein adopted a compact three-dimensional structure at pH 4.5. Colony following unit (CFU) inhibition assay demonstrated that 25 mu M fusion protein at pH 7.4 had all anti microbial activity of 40% against E. coli K12D31. which might imply the fusion protein functions as multimeric states. In conclusion the GB1 fusion partner helps BIN1b form a stable homogenous conformation to facilitate subsequent structural determination Without a significant effect oil the antimicrobial activity. (c) 2008 Elsevier B.V. All rights reserved. |
| WOS关键词 | HIGH-LEVEL EXPRESSION ; ESCHERICHIA-COLI ; BETA-DEFENSIN ; PROTEIN ; SYSTEM |
| 资助项目 | Chinese Academy of Sciences (CAS) Knowledge Creative Program[KSM-M-R-54] ; Chinese Academy of Sciences (CAS) Knowledge Creative Program[KSCX2-YW-R-104] ; National Natural Science Foundation of China[30570352] ; National Natural Science Foundation of China[30730026] ; Shanghai Science and Technology Committee[07ZR14135] |
| WOS研究方向 | Biotechnology & Applied Microbiology |
| 语种 | 英语 |
| WOS记录号 | WOS:000262795600006 |
| 出版者 | ELSEVIER SCIENCE BV |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/279393]  |
| 专题 | 分析化学研究室 |
| 通讯作者 | Lin, Donghai |
| 作者单位 | 1.Shanghai Inst Planned Parenthood Res, Shanghai 200032, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Biol Sci, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China; 3.Chinese Acad Sci, Inst Biochem & Cell Biol, Shanghai Inst Biol Sci,State Key Lab Mol Biol, Shanghai Key Lab Mol Androl, Shanghai 200031, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Guo, Chenyun,Diao, Hua,Lian, Yandong,et al. Recombinant expression and characterization of an epididymis-specific antimicrobial peptide BIN1b/SPAG11E[J]. JOURNAL OF BIOTECHNOLOGY,2009,139(1):33-37. |
| APA | Guo, Chenyun.,Diao, Hua.,Lian, Yandong.,Yu, Heguo.,Gao, Hongchang.,...&Lin, Donghai.(2009).Recombinant expression and characterization of an epididymis-specific antimicrobial peptide BIN1b/SPAG11E.JOURNAL OF BIOTECHNOLOGY,139(1),33-37. |
| MLA | Guo, Chenyun,et al."Recombinant expression and characterization of an epididymis-specific antimicrobial peptide BIN1b/SPAG11E".JOURNAL OF BIOTECHNOLOGY 139.1(2009):33-37. |
入库方式： OAI收割
来源：上海药物研究所
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