Candida albicans is the most common human fungal pathogen in immunocompromised individuals. With the emergence of clinical fungal resistance, there is an urgent demand to develop novel antifungal agents. The antibacterial peptide (AMP) is an important component in the innate immune system and has a good therapeutic effect on patients infected with microorganisms. AMP-17, a novel AMP from Musca domestica, has an antifungal effect against C. albicans, but the mechanism of antifungal action remains unclear. In this study, we performed proteomic analysis of C. albicans treated AMP-17 and No drug using a combination of a series of cutting-edge technologies, including TMT labeling, HPLC classification and quantitative proteomics based on mass spectrometry. A total of 3,931 proteins were identified, of which 3,600 contained quantitative information. With a 1.5-fold change threshold and a t-test p-value <0.05 as a standard, 423 differentially expressed proteins (DEPs) were up-regulated and 180 differentially expressed proteins (DEPs) were down-regulated in the quantitative AMP_17/con comparison group. In these DEPs, proteins associated with ergosterol biosynthesis, oxidative stress and cell wall were identified as significantly up-regulated, while proteins involved in fatty acid biosynthesis were identified as significantly down-regulated. In addition, using the KEGG enrichment assay, seven significant KEGG pathways were identified, primarily involved in oxidative phosphorylation, propionic acid metabolism, and fatty acid metabolism. These results showed that AMP-17 induces a complex organism response to C. albicans, indicating that AMP-17 can inhibit growth by affecting multiple targets in C. albicans cells.