The document describes a study that aimed to destabilize the bacterial accumulation associated protein (AAP) in order to modify its antigen recognition and reduce biofilm production. Researchers mutated the amino acid phenylalanine-20 in the AAP's G5 repeat domain to alanine using site-directed mutagenesis. This was intended to destabilize the hydrophobic core of G5 and improve its presentation as an antigen to the immune system. The mutated AAP-G5 peptide will be tested in mice to examine the immune response. While the researchers successfully extracted and isolated the pET21a+ vector containing the mutated gene, their initial mutagenesis and transformation of the pVAX plasmid was unsuccessful. Future plans are to