Autophagy is a self-degradative process in eukaryotic cells that facilitates the breakdown of cellular components within lysosomes. Autophagy is broadly classified into three types: macroautophagy, microautophagy, and chaperone-mediated autophagy (CMA). In CMA, the chaperone protein heat shock cognate 71 kDa (HSC70) recognizes a specific pentapeptide motif, known as the KFERQ-like motif, within substrate proteins and facilitates their targeted degradation in lysosomes. In this study, we designed and synthesized a series of conjugates by combining a CMA-targeting ligand based on the KFERQ-like motif with a ligand specific for the target protein BRD4, such as JQ1. JQ1 was conjugated either to the N-terminal or the C-terminal end of the peptide sequences containing the KFERQ-like motif. HeLa cells were treated with various concentrations of these CMA-targeting conjugates, and BRD4 degradation efficiency was assessed in different times. We found that the JQ1 conjugated LDRLQ sequence can degrade BRD4 with DC₅₀ value approximately 50 µM. The degradation efficiency was also significant after 6 hours of treatment in HeLa cells. The cell viability assay showed that all of the peptide sequences have no toxicity to HeLa cells. In addition, we tested the cell penetration capacity by labeling the peptide sequences with TAMRA and estimated the fluorescence intensity. The results indicated that the peptides penetrate into HeLa cells with EC₅₀ value of 5.8 µM. Future studies will focus on optimizing the peptide sequences to maximize their efficacy in BRD4 degradation.