Two individuals of Odorrana hosii were collected from Sungai Sedim Recreational Forest, Kedah, Peninsular Malaysia. Both specimens were observed resting on wet, moss-covered rocks at the edge of the main river. Skin secretions were extracted and transported to the laboratory for further analysis. In the laboratory, the secretions were freeze-dried, quantified for protein concentration, and analyzed using Liquid Chromatography–Tandem Mass Spectrometry (LC-MS/MS). The Pierce assay revealed a protein concentration of 0.1167 mg/mL. Based on the Universal Protein Resource (UniProt) amphibian database, 43 proteins were identified, comprising 28 (65%) antimicrobial peptides (AMPs), 5 (12%) uncharacterized proteins, and 10 (23%) other proteins. The 28 AMPs belonged to 13 distinct families, including esculentin-2 (5 peptides, 18%), esculentin-1 (3 peptides, 11%), brevinin-1 (3 peptides, 11%), brevinin-2 (3 peptides, 11%), andersonin-C (2 peptides, 7%), nigrocin-2 (2 peptides, 7%), palustrin-2 (2 peptides, 7%), odorranian-C (2 peptides, 7%), tiannanensin (2 peptides, 7%), and four peptides (14%) from other AMP families. These AMPs warrant further investigation to determine their potential activity against pathogenic microorganisms.