# Unveiling the Potential Binding Targets of Celastrol in Colorectal Cancer: A Proteomic Profiling Approach Integrating Cellular Thermal Shift Assay and Pulse Proteolysis

## TL;DR

This study identifies eight potential protein targets of celastrol in colorectal cancer using proteomic techniques, offering new insights for drug development.

## Contribution

A novel method combining cellular thermal shift assay and pulse proteolysis is used to identify celastrol's binding targets in colorectal cancer.

## Key findings

- Eight potential binding proteins of celastrol were identified using proteomic profiling.
- The identified proteins include EEF2, STIP1, GAPDH, FLNA, SETSIP, GANAB, TXNDC17, and PRDX2.
- The findings offer new avenues for targeted therapies in colorectal cancer.

## Abstract

Celastrol, a natural compound classified as a pentacyclic
triterpenoid,
has demonstrated efficacy in inhibiting human colorectal cancer cells’
growth, adhesion, and metastasis through various signaling pathways.
However, the specific protein target responsible for the effects of
celastrol remains unclear, limiting its potential for further applications
in colon cancer treatment and drug development. In this study, we
propose a novel approach by combining a cellular thermal shift assay
and pulse proteolysis techniques to identify the potential binding
proteins of celastrol. Utilizing proteomic profiling on 2-dimensional
electrophoresis, we successfully identified eight potential binding
targets. MALDI-TOF mass spectrometry was conducted to verify these
proteins as EEF2, STIP1, GAPDH, FLNA, SETSIP, GANAB, TXNDC17, and
PRDX2. Our results provide valuable insights into the protein targets
through which celastrol exerts its pharmacological effects, opening
up new avenues for targeted therapies and drug development in colorectal
cancer.