S-100 α chain Inhibitors

SB-3CT achieves inhibition of the S-100A4 protein by directly binding to its active site, which blocks the protein's ability to interact with target molecules involved in metastasis, effectively impeding cancer cell migration and invasion.r.

Piceatannol disrupts the biochemical interaction between S-100B and p53 by competing for the binding site on S-100B that is crucial for the interaction with p53, thereby preserving p53's tumor-suppressive functions.

Nordihydroguaiaretic Acid (NDGA) binds to S-100B and alters its conformation, which in turn inhibits the protein's ability to bind calcium ions and interact with downstream signaling molecules, leading to neuroprotective effects.

Carvedilol directly interacts with S-100A1, blocking its calcium-binding sites and thus inhibiting the protein's capacity to modulate calcium signaling in cardiomyocytes, which is crucial for cardiac function.

Pentamidine interferes with the calcium-binding domain of S-100A6, preventing the protein from undergoing conformational changes necessary for its interaction with target proteins involved in cell cycle regulation and apoptosis.

Zinc exerts its inhibitory effect on S-100A12 by binding to the protein's calcium-binding sites, preventing the proper folding and function of S-100A12, and thus diminishing its role in inflammatory responses.

Ethyl Pyruvate blocks the activation of the S-100A8/A9 complex by interfering with its ability to bind calcium, which is crucial for the complex's pro-inflammatory signaling activities.

Amlexanox inhibits the interaction between S-100A4 and nonmuscle myosin IIA by binding to S-100A4, disrupting its ability to interact with and modulate the function of nonmuscle myosin IIA, affecting cell motility.

Curcumin inhibits the expression of S-100A4 by interfering with the transcription factors or signaling pathways that regulate S-100A4 gene expression, leading to a decrease in the levels of S-100A4 protein and its associated metastatic potential.