Structure-based and in silico design of Hsp90 inhibitors.
The molecular chaperone Hsp90 is responsible for activation and stabilization of several oncoproteins in cancer cells, and has emerged as an important target in cancer treatment because of this pivotal role. In recent years, interests have arisen around structure-based design of small molecules aimed at inhibiting the chaperone activity of Hsp90. In this review, we illustrate the recent advances in structure-based and in silico strategies aimed at discovering and optimizing Hsp90 inhibitors.
Sgobba
Miriam
M
Dipartimento di Scienze Farmaceutiche, University of Modena and Reggio Emilia, Via Campi 183, 41100 Modena, Italy.
Rastelli
Giulio
G
D049933:Aminocoumarins / Q000737:chemistry / Q000494:pharmacology; D000970:Antineoplastic Agents / Q000737:chemistry* / Q000494:pharmacology; D001393:Azoles / Q000737:chemistry / Q000494:pharmacology; D016227:Benzoquinones / Q000737:chemistry / Q000494:pharmacology; D015195:Drug Design; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors* / Q000378:metabolism; D047029:Lactams, Macrocyclic / Q000737:chemistry / Q000494:pharmacology; D018942:Macrolides / Q000737:chemistry / Q000494:pharmacology; D011687:Purines / Q000737:chemistry / Q000494:pharmacology; D013329:Structure-Activity Relationship
D049933:Aminocoumarins; D000970:Antineoplastic Agents; D001393:Azoles; D016227:Benzoquinones; D018841:HSP90 Heat-Shock Proteins; D047029:Lactams, Macrocyclic; D018942:Macrolides; D011687:Purines; C035359:monorden; C001277:geldanamycin