Chemical Proteomics Reveals Heat Shock Protein 60 To Be the Main Cellular Target of the Marine Bioactive Sesterterpene Suvanine

被引：20

作者：

Cassiano, Chiara ^{[1
]}

Monti, Maria Chiara ^{[1
]}

Festa, Carmen ^{[2
]}

Zampella, Angela ^{[2
]}

Riccio, Raffaele ^{[1
]}

Casapullo, Agostino ^{[1
]}

机构：

[1] Univ Salerno, Dipartimento Sci Farmaceut & BioMed, I-84084 Salerno, Italy

[2] Univ Naples Federico II, Dipartimento Chim Sostanze Nat, I-80131 Naples, Italy

来源：

CHEMBIOCHEM | 2012年 / 13卷 / 13期

关键词：

heat shock protein 60; inhibitors; marine sesterterpene; mass spectrometry; proteomics; SPONGE COSCINODERMA-MATHEWSI; HEAT-SHOCK PROTEINS; NATURAL-PRODUCTS; MOLECULAR CHAPERONES; CITRATE SYNTHASE; INHIBITOR; BINDING; HSP60;

D O I：

10.1002/cbic.201200291

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1953 / 1958

页数：6

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