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	Display of aggregation-prone ligand binding domain of human ppar gamma on surface of bacteriophage lambda
	Kong, B; Ma, WJ
刊名	Acta pharmacologica sinica
	2006
卷号	27期号:1页码:91-99
关键词	Protein expression Lambda phage Surface display Nuclear receptor Peroxisome proliferator-activated receptors Ligand binding domain
ISSN号	1671-4083
DOI	10.1111/j.1745-7254.2006.00253.x
通讯作者	Ma, wj(wjma@sibs.ac.cn)
英文摘要	Aim: to display the aggregation-prone ligand binding domain (lbd) of the human peroxisome proliferator-activated receptor gamma (ppar gamma) on the surface of bacteriophages to establish an easy screening assay for the identification of ppar gamma ligands. methods: plasmids were constructed for the expression of the ppar gamma lbd as a fusion to the n-terminus of the g3p protein of filamentous phage or the c-terminus of the capsid protein d (pd) of phage lambda. the fusion proteins were expressed in e coli and solubility characteristics were compared. polyclonal antibodies against the lbd as well as the pd protein were prepared for western blot analysis and phage capture assay. results: the pd-lbd fusion protein was partially soluble, whereas the lbd-g3p fusion protein was detected only in the insoluble fraction. the pd-lbd fusion protein was efficiently incorporated in phage particles. furthermore, the lbd was shown to be displayed on the surface of bacteriophage lambda. on average, the pd-lbd fusion protein accounted for 28% of the total pd protein in the lambda head capsid. conclusion: the hydrophobic ppar gamma lbd was expressed as a soluble form of fusion protein in e coli and displayed on the surface of bacteriophage lambda when it was fused to the lambda pd protein. the lambda pd fusion system could be used for improving the solubility of proteins that tend to form inclusion bodies when expressed in e coli. the lambda phage particles displaying the lbd of ppar gamma may be of great value for the identification of novel ppar gamma ligands.
WOS关键词	NUCLEAR RECEPTOR SUPERFAMILY ; ESCHERICHIA-COLI ; PHAGE DISPLAY ; LIPID-METABOLISM ; CDNA LIBRARIES ; PROTEIN D ; EXPRESSION ; FUSION ; PURIFICATION ; SELECTION
WOS研究方向	Chemistry ; Pharmacology & Pharmacy
WOS类目	Chemistry, Multidisciplinary ; Pharmacology & Pharmacy
语种	英语
出版者	ACTA PHARMACOLOGICA SINICA
WOS记录号	WOS:000234427200009
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2379544
专题	中国科学院大学
通讯作者	Ma, WJ
作者单位	1.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Hlth Sci, Shanghai 200025, Peoples R China 2.Shanghai Jiao Tong Univ, Sch Med, Shanghai 200025, Peoples R China 3.Chinese Acad Sci, Shanghai Inst Biol Sci, Shanghai Res Ctr Biotechnol, Shanghai 200233, Peoples R China 4.Chinese Acad Sci, Grad Sch, Beijing 100864, Peoples R China
推荐引用方式 GB/T 7714	Kong, B,Ma, WJ. Display of aggregation-prone ligand binding domain of human ppar gamma on surface of bacteriophage lambda[J]. Acta pharmacologica sinica,2006,27(1):91-99.
APA	Kong, B,&Ma, WJ.(2006).Display of aggregation-prone ligand binding domain of human ppar gamma on surface of bacteriophage lambda.Acta pharmacologica sinica,27(1),91-99.
MLA	Kong, B,et al."Display of aggregation-prone ligand binding domain of human ppar gamma on surface of bacteriophage lambda".Acta pharmacologica sinica 27.1(2006):91-99.

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