Structure-based design of HSPA5 inhibitors: From peptide to small molecule inhibitors
M Huang, Z Li, D Li, S Walker, C Greenan… - Bioorganic & medicinal …, 2013 - Elsevier
M Huang, Z Li, D Li, S Walker, C Greenan, R Kennedy
Bioorganic & medicinal chemistry letters, 2013•ElsevierWe identified nine small-molecule hit compounds of Heat shock 70kDa protein 5 (HSPA5)
from cascade in silico screening based on the binding modes of the tetrapeptides derived
from the peptide substrate or inhibitors of Escherichia coli HSP70. Two compounds exhibit
promising inhibition activities from cancer cell viability and tumor inhibition assays. The
binding modes of the hit compounds provide a platform for development of selective small
molecule inhibitors of HSPA5.
from cascade in silico screening based on the binding modes of the tetrapeptides derived
from the peptide substrate or inhibitors of Escherichia coli HSP70. Two compounds exhibit
promising inhibition activities from cancer cell viability and tumor inhibition assays. The
binding modes of the hit compounds provide a platform for development of selective small
molecule inhibitors of HSPA5.
We identified nine small-molecule hit compounds of Heat shock 70kDa protein 5 (HSPA5) from cascade in silico screening based on the binding modes of the tetrapeptides derived from the peptide substrate or inhibitors of Escherichia coli HSP70. Two compounds exhibit promising inhibition activities from cancer cell viability and tumor inhibition assays. The binding modes of the hit compounds provide a platform for development of selective small molecule inhibitors of HSPA5.
Elsevier