DsbA enzymes catalyze oxidative folding of multiple classes of virulence factors in Gram-negative bacteria. The development of antivirulence drugs, which block virulence factors in pathogens instead of killing or inhibiting the growth of pathogens, is a possible solution to the global threat of antimicrobial resistance, making DsbA an attractive antibacterial drug target. In this study, 34 small molecule DsbA inhibitors, found in literature, were analyzed and evaluated, using a computational approach. Molecular docking of the inhibitors to EcDsbA (Escherichia coli DsbA), VcDsbA (Vibrio cholerae DsbA) and SeDsbA (Salmonella enterica serovar Typhimurium DsbA) was performed and two inhibitors demonstrated significantly higher overall binding affinity. Investigation of these two inhibitors showed that the stability of the DsbA-inhibitor complexes could be further increased, by modifying the inhibitors. One modified inhibitor gave rise to higher binding energy as compared to its precursor inhibitor for all three DsbA proteins. This is a promising result, indicating that non-specific pathogen DsbA inhibitors can be developed, despite the structural differences in active sites between EcDsbA, VcDsbA and SeDsbA. This work highlights the capacity of in silico methods to identify and optimize novel compounds which could serve as a starting point for the development of antivirulence drugs.