Tumor selectivity of Hsp90 inhibitors: the explanation remains elusive.
Two recent papers attempt to solve both the tumor selectivity and the in vivo tumor accumulation profiles seen with some Hsp90 inhibitors. They spotlight the higher affinity of ansamycins' hydroquinone over the quinone form for Hsp90 and further discuss its possible contribution to ansamycins' tumor selectivity.
Chiosis
Gabriela
G
Department of Medicine and Program in Molecular Pharmacology and Chemistry, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, New York 10021, USA.
Neckers
Len
L
D000818:Animals; D000970:Antineoplastic Agents / Q000008:administration & dosage* / Q000145:classification / Q000494:pharmacology*; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors* / Q000502:physiology*; D006801:Humans; D009369:Neoplasms / Q000188:drug therapy* / Q000378:metabolism* / Q000473:pathology
D000970:Antineoplastic Agents; D018841:HSP90 Heat-Shock Proteins