molecular chaperone

TRC051384 is a heat shock protein 70 (HSP70) inducer that reduces stroke-associated neuronal damage and increases survival in a rat model of transient ischemic stroke, activates heat shock factor-1 and leads to elevated molecular chaperone and anti-inflammatory activity, and enhances Hsp72 expression in neurons and glial cells.

Tamoxifen-d5 is a deuterium labeled Tamoxifen. Tamoxifen is a selective modulator of estrogen receptor (SERM). Tamoxifen is a potent activator of Hsp90 and enhances the Hsp90 molecular chaperone ATPase activity.

MAL3-101 is a molecular chaperone inhibitor of heat shock protein 70 (Hsp 70).

Claficapavir (A1752) is a potent nucleocapsid protein (NC) inhibitor that effectively binds the HIV-1 NC with a dissociation constant (Kd) of 20 nM, resulting in the inhibition of its chaperone properties. This specific molecular interaction leads to strong antiviral activity against HIV-1, with an IC50 of approximately 1 μM [1].

BIIB028 is a small-molecule inhibitor of heat shock protein (Hsp) 90 with potential antineoplastic activity. Hsp90 inhibitor BIIB028 blocks the binding of oncogenic client proteins to Hsp90, which may result in the proteasomal degradation of these proteins and so the inhibition of tumor cell proliferation. Hsp90 is a molecular chaperone that plays a key role in the conformational maturation of oncogenic signaling proteins, such as Her2 Erbb2, Akt, Raf1, Bcr-Abl, and mutated p53, in addition to other molecules involved in cell cycle regulation and immune responses.

O-Carboranylphenoxyacetanilide is an HIF-1α inhibitor that suppresses the activation of HIF-1α. It inhibits the transcriptional activity of HIF in HeLa cells (IC50: 0.74 μM) and also suppresses the molecular chaperone activity of HSP60 as well as the HSP60 ATPase activity.

Versipelostatin, a GRP78 Bip molecular chaperone down-regulator, can be isolated from the culture broth of Streptomyces versipellis 4083-SVS6 [1].

HSP70 DnaK substrate peptide is a short peptide segment that binds to and interacts with the HSP70 DnaK molecular chaperone. It is utilized to investigate the functional mechanisms of HSP70 DnaK in molecular chaperone activity.