atpase activity

S-trityl-L-Cysteine is a non-natural amino acid and an inhibitor of Eg5, also known as KSP and Kif11, a mitotic kinesin necessary for mitotic spindle formation. S-trityl-L-Cysteine inhibits the ATPase activity of Eg5 in basal and microtubule-stimulated states (IC50s = 1,000 and 140 nM, respectively). It is selective for Eg5 over nine other human kinesins in an enzyme-coupled assay. It reversibly inhibits Eg5-driven microtubule sliding velocity with an IC50 value of 500 nM using X. laevis recombinant Eg5. It induces cell cycle arrest in HeLa cells (IC50 = 700 nM), reversibly halting the cell cycle in the mitotic phase by inhibiting the separation of duplicated chromosomes and preventing bipolar spindle formation. S-trityl-L-Cysteine inhibits the growth of cancer cells in vitro when tested against the National Cancer Institute (NCI) 60 human cancer cell line panel (average GI50 = 1.3 μM) and in mouse xenograft models.

Reversin 121, a P-glycoprotein inhibitor, enhances MDR1's ATPase activity and counteracts P-glycoprotein-mediated multidrug resistance, making it useful in cancer research.

C-Peptide 1 (rat) is a polypeptide isolated from proinsulin. C-Peptide acts as a β-catenin/GSK-3β activator, influences Na/K-ATPase activity, regulates apoptosis, and may improve diabetic neuropathy.

Aurein 2.3, an antibiotic antimicrobial peptide, partially inhibits E. coli ATPase activity and suppresses cell growth [1] [2].

Caloxin 1b3 is a peptide and a selective inhibitor of the plasma membrane calcium pump 1 (PMCA1). It demonstrates a stronger inhibitory effect on the Ca2+–Mg2+-ATPase activity of PMCA1 in rabbit duodenal mucosa compared to PMCA4 in human erythrocyte ghosts. Additionally, Caloxin 1b3 increases cytoplasmic Ca2+ levels in endothelial cells and is useful in cardiovascular disease research.