Chemical Synthesis of the N-Terminal Cysteine-Rich Domain of Human OX40

摘要

The human OX40 receptor (hOX40) is a transmembrane protein that is part of the tumor necrosis factor receptor superfamily (TNFRSF). The extracellular region of hOX40 is composed of approximately 3.5 cysteine-rich domains (CRDs). Molecules that bind to hOX40 and modulate receptor signaling could be used to treat autoimmune diseases, inflammation, and cancer [1]. The N-terminal domain of some TNFRSF members is implicated in receptor self-association in the absence of ligand [2]. We report the synthesis of a biotinylated analogue of the 36-residue N-terminal CRD of hOX40 (CRD-Biotin) to evaluate the function of this domain.