Human neutrophil elastase (HNE) is a serine protease released by inflammatory stimuli. In normal conditions this enzyme activity is controlled by endogenous inhibitors, but with the continuous activation of inflammatory cells, and consequent release of HNE, the endogenous inhibition is not enough. The uncontrolled HNE activity is related to various inflammatory chronic diseases, such as psoriasis, rheumatoid arthritis and chronic obstructive pulmonary disease. It is also related to the wound healing process, the presence of high levels of HNE has been implicated in tissue damage. Consequently, the interest in researching HNE inhibitors has been raised. Indeed, therapeutic peptides with antimicrobial features have been uncovered as potential strategies in this fight. In this sense, here, we explore the antibacterial properties of the tetrapeptide Ala-Ala-Pro-Val (AAPV), known for ability to inhibit HNE activity. AAPV peptide was synthesized by means of microwave-assisted solid phase peptide synthesis, using a chlorotritylchloride solid support, a 9-fluorenylmethoxycarbonyl α-amino protection, and N,N′-diisopropylcarbodiimide/Ethyl cyanoglyoxylate-2-oxime to guarantee coupling reactions. The peptide, obtained in a yield of about 58%, was considered pure after analytical high performance liquid chromatography and the respective structure confirmed by two-dimensional nuclear magnetic resonance spectroscopy. Its antimicrobial potential was explored via minimum inhibitory concentration evaluations against some of the most common pathogens colonizing chronic wounds, namely Staphylococcus aureus, Staphylococcus epidermidis (Gram-positive), Pseudomonas aeruginosa and Escherichia coli (Gram-negative). The peptide only has demonstrated activity at 2mg/mL, which is too high for a cost-effective application.