Analysis Interactions of IDO1 and Inhibitors by Microscale Thermophoresis (MST) (CAT#: STEM-MB-2470-LGZ)

Introduction

L-tryptophan (L-Trp) catabolism has attracted attention due to its importance in immunity. 95% of dietary L-tryptophan is broken down via the kynurenine pathway (KP), in which IDO1 is a heme-containing enzyme that catalyzes the first and rate-limiting step of the pathway to generate N-formyl kynurine acid. Many downstream products of KP have been identified as bioactive compounds, showing the ability to modulate inflammatory responses through multiple mechanisms. Therefore, accumulating evidence makes IDO1 a key drug target for controlling the balance between immune tolerance and immune inflammatory responses. Inhibition of IDO1 is a strategy in the immuno-oncology pipeline for the development of novel anticancer therapies. By studying the specific binding characteristics of different inhibitors to IDO1, clues can be provided for the design of next-generation enzyme inhibitors.