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Title 

Proteomimetic libraries: design, synthesis, and evaluation of p53-MDM2 interaction inhibitors

Authors 

F LuSeung-Wook ChiDo-heyoung KimKyou Hoon HanI D KuntzR K Guy

Publisher 

American Chemical Society

Issue Date 

2006

Citation 

Journal of Combinatorial Chemistry, vol. 8, no. 3, pp. 315-325

Keywords 

enzyme inhibitorprotein MDM2protein p53drug designevaluationsynthesisenzyme inhibitorsproto-oncogene proteins c-mdm2tumor suppressor protein p53

Abstract 

The p53-MDM2 interaction regulates p53-mediated cellular responses to DNA damage, and MDM2 is overexpressed in 7% of all cancers. Structure-based computational design was applied to this system to design libraries centered on a scaffold that projects side chain functionalities with distance and angular relationships equivalent to those seen in the MDM2 interacting motif of p53. A library of 173 such compounds was synthesized using solution phase parallel chemistry. The in vitro competitive ability of the compounds to block p53 peptide binding to MDM2 was determined using a fluorescence polarization competition assay. The most active compound bound with Kd = 12 μM, and its binding was characterized by 15N-1H HSQC NMR.

ISSN 

1520-4766

Link 

http://dx.doi.org/10.1021/cc050142v

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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