Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-34628
Melkko, S; Mannocci, L; Dumelin, C E; Villa, A; Sommavilla, R; Zhang, Y; Grütter, M; Keller, N; Jermutus, L; Jackson, R H; Scheuermann, J; Neri, D (2010). Isolation of a small-molecule inhibitor of the antiapoptotic protein Bcl-xL from a DNA-encoded chemical library. ChemMedChem, 5(4):584-590.
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Bcl-xL is an antiapoptotic member of the Bcl-2 protein family and an attractive target for the development of anticancer agents. Here we describe the isolation of binders to Bcl-xL from a DNA-encoded chemical library using affinity-capture selections and massively parallel high-throughput sequencing of >30,000 sequence tags of library members. The most potent binder identified, compound 19/93 [(R)-3-(amido indomethacin)-4-(naphthalen-1-yl)butanoic acid], bound to Bcl-xL with a dissociation constant (K(d)) of 930 nM and was able to compete with a Bak-derived BH3 peptide, an antagonist of Bcl-xL function.
|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > Institute of Biochemistry|
07 Faculty of Science > Institute of Biochemistry
|DDC:||570 Life sciences; biology|
|Date:||06 April 2010|
|Deposited On:||06 Jul 2010 10:27|
|Last Modified:||12 Jan 2014 17:47|
|Citations:||Web of Science®. Times Cited: 10|
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