Berberine inhibits arylamine N-acetyltransferase activity and gene expression in Salmonella typhi

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Title:	Berberine inhibits arylamine N-acetyltransferase activity and gene expression in Salmonella typhi
Authors:	Wu, LT;Tsou, MF;Ho, CC;Chuang, JY;Kuo, HM;Chung, JG
Contributors:	健康照護學院醫技系;China Med Univ, Dept Med, Lab Sci & Biotechnol, Taichung 404, Taiwan;China Med Univ, Dept Parasitol, Taichung 404, Taiwan;China Med Univ, Dept Microbiol, Taichung 404, Taiwan;China Med Univ Hosp, Dept Internal Med, Taichung 404, Taiwan;Chungtai Inst Hlth Sci & Technol, Dept Nursing, Taichung, Taiwan
Date:	2005
Issue Date:	2010-09-24 14:38:57 (UTC+8)
Publisher:	SPRINGER
Abstract:	The growth factor receptor-binding protein-Src homology 2 (Grb2-SH2) domain plays an important role in the oncogenic Ras signal transduction pathway, which involves cell proliferation and differentiation. Therefore, the Grb2-SH2 domain has been chosen as our target for development of potential antiproliferative agents. Herein, we report the study of the inhibitory effects of small nonphosphorylated peptide analogs interacting with the Grb2-SH2 domain protein by surface plasmon resonance (SPR) technology. A set of 8 related peptide analogs were synthesized, purified, and characterized. Their inhibitory effects on Grb2-SH2 were evaluated by the SPR technology developed with the BIACORE X instrument. The lead peptide, Fmoc-Glu-Tyr-Aib-Asn-NH2 (Fmoc-E-Y-Aib-N,- Fmoc: 9-fluorenylmethyoxycarbonyl; Aib = alpha-amino isobutyric acid) inhibited Grb2-SH2 domain function with an IC50 value of 8.7 mu M. A molecular modeling study of the lead peptide indicated that the glutamate in the Fmoc peptide is ideally positioned to form a strong salt bridge to Arg 67 in the Grb2-SH2 domain, using both its backbone carbonyl and its acidic group. Residue Glu 89 in Grb2-SH2 flips inward to fill the binding site and partially replace the phosphate group as a hydrogen-bond acceptor. Results of these studies provide important information for further development of potent nonphosphorylated peptide inhibitors of the Grb2-SH2 domain. (C) 2005 Wiley Periodicals, Inc.
Relation:	CURRENT MICROBIOLOGY 51(4):255-261
Appears in Collections:	[Department of Medical Laboratory Science and Biotechnology ] Journal articles

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