Natural product inhibitors of Hsp90: potential leads for drug discovery

Abstract

Heat shock protein 90 has emerged as a promising target for the treatment of cancer and neurodegenerative diseases. This review summarizes recent advancements towards the development of natural products as they pertain to the biological and chemical understanding of this molecular chaperone.

Fig. (1)

Structure of geldanamycin.

Fig. (2)

The protein folding mechanism of Hsp90.

Fig. (3)

The effects of lysosomal pH on cellular drug distribution.

Fig. (4)

Structures of 17-AAG and AEG3482.

Fig. (5)

Structures of geldanamycin, structural analogues 17-AAG and 17-DMAG, and herbimycin.

Fig. (6)

Structures of radicicol, c-RDC, KF25706 and Pochonin A & D.

Fig. (7)

Structure of the chimeric analogues of Geldanamycin and Radicicol.

Fig. (8)

The coumermycin family of antibiotics.

Fig. (9)

Structures of novobiocin analogues.

Figure 10

Structure of EGCG.

Fig. (11)

The structure of taxol.

Fig. (12)

Structure of Derrubone.

Fig. (13)

Structures of Gedunin and Celastrol.