Linking bioactive compounds to their cellular targets is a central challenge in chemical biology. Herein we report the mode of action of perthamide C, a natural cyclopeptide isolated from the marine sponge Theonella swinhoei. Through an emerging mass spectrometry-based chemical proteomics approach, Heat Shock Protein 90 and Glucose Regulated Protein 94 were identified as key targets of perthamide C and this evidence has been validated using surface plasmon resonance. The ability of perthamide C to influence heat shock protein-mediated cell apoptosis revealed that this marine metabolite could be a good candidate for the development of a lead compound with therapeutic applications based on apoptosis modulation.
Heat Shock Proteins as Key Biological Targets of the Marine Natural Cyclopeptide Perthamide C / L., Margarucci; M. C., Monti; A., Mencarelli; S., Fiorucci; R., Riccio; Zampella, Angela; A. C. a. s. a. p. u. l. l., O.. - In: MOLECULAR BIOSYSTEMS. - ISSN 1742-206X. - 8:5(2012), pp. 1412-1417. [10.1039/c2mb05507d]
Heat Shock Proteins as Key Biological Targets of the Marine Natural Cyclopeptide Perthamide C
M. C. Monti;ZAMPELLA, ANGELA;
2012
Abstract
Linking bioactive compounds to their cellular targets is a central challenge in chemical biology. Herein we report the mode of action of perthamide C, a natural cyclopeptide isolated from the marine sponge Theonella swinhoei. Through an emerging mass spectrometry-based chemical proteomics approach, Heat Shock Protein 90 and Glucose Regulated Protein 94 were identified as key targets of perthamide C and this evidence has been validated using surface plasmon resonance. The ability of perthamide C to influence heat shock protein-mediated cell apoptosis revealed that this marine metabolite could be a good candidate for the development of a lead compound with therapeutic applications based on apoptosis modulation.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
