This peptide sequence is primarily utilized in biochemical research, particularly in studies involving cell adhesion and signaling pathways. The aspartic acid residues in the sequence mimic the natural binding sites for calcium ions, making it useful in experiments focused on calcium-dependent processes. It is often employed in assays to investigate integrin-mediated cell adhesion, as the sequence resembles motifs found in extracellular matrix proteins. Additionally, the lysine residue provides a positive charge, facilitating interactions with negatively charged molecules or surfaces. The bNA (benzoyl-naphthylalanine) group enhances fluorescence properties, making it suitable for tracking and imaging applications in cellular studies. Its ammonium salt form ensures solubility in aqueous solutions, which is essential for in vitro experiments.