Chloroacetylation of cyclostreptin influences its interaction with tubulin

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Title:	Chloroacetylation of cyclostreptin influences its interaction with tubulin
Authors:	Calvo, Enrique; Barasoain, Isabel CSIC ; Camafeita, Emilio; Andreu, José Manuel CSIC ORCID ; López, Juan Antonio; Díaz, José Fernando CSIC ORCID
Issue Date:	2009
Publisher:	Sociedad Española de Proteómica Universidad de Navarra
Citation:	Proteómica: revista de la Sociedad Española de Proteómica 3: 86 (2009)
Abstract:	Cyclostreptin (Cs) is a natural product from Streptomyces sp.9885 that irreversibly stabilizes cellular microtubules by covalent binding to tubulin, causes cell cycle arrest, evades drug resistance in MDR tumor cells and inhibits paclitaxel-binding to microtubules. In a previous work (1) we demonstrated that cyclostreptin irreversibly binds to β-tubulin through Thr220 and Asn228 (the type-I pore binding site). To gain further information about this binding site, two reactive derivatives of cyclostreptin were synthesized and studied.
Description:	Resumen del trabajo presentado en el 3rd Congress of the Spanish Proteomics Society (SEProt) and 2nd Latin American Human Proteome Organisation, celebrado en Pamplona (España), del 10 al 13 de febrero de 2009
Publisher version (URL):	http://www.seprot.es/wp-content/uploads/2016/05/Proteomica_Vol3_Feb09.pdf
URI:	http://hdl.handle.net/10261/251220
ISSN:	1888-0096
Appears in Collections:	(CIB) Artículos