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Chemical Proteomics Reveals Heat Shock Protein 60 To Be the Main Cellular Target of the Marine Bioactive Sesterterpene Suvanine
Author(s) -
Cassiano Chiara,
Monti Maria Chiara,
Festa Carmen,
Zampella Angela,
Riccio Raffaele,
Casapullo Agostino
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200291
Subject(s) - interactome , proteomics , heat shock protein , chemical biology , chaperone (clinical) , chemistry , computational biology , proteome , heat shock , biology , microbiology and biotechnology , biochemistry , medicine , pathology , gene
Marine bioactive compounds are potential drug leads because of their diverse pharmacological effects against human diseases. The identification of their cellular targets is crucial for a rational approach to their application in medicinal chemistry. Thus, we have analyzed the cell interactome of suvanine, a sulfated tricyclic terpenoid of marine origin endowed with an interesting anti‐inflammatory activity, by application of a chemical proteomic approach. Heat Shock Protein 60, a chaperone involved in the inflammatory response, is the main cellular target of suvanine, which is also able to interfere with protein chaperone activity, giving evidence for its anti‐inflammatory properties.