<![CDATA[Introduction: Oral cancer is the 11th most common cancer worldwide. Previous studies have reported that saliva contains biomarkers for oral cancer. MMP-9, found in saliva, is a marker that indicates and facilitates tumor development. However, comprehensive biomolecular and bioinformatics characterization of salivary MMP-9 remains limited. This study aimed to analyze the biomolecular and bioinformatics characteristics of salivary MMP-9 as an oral cancer biomarker and a potential target for therapy because it plays an important role in tumor development and management. Methods: The features of MMP-9 were obtained from the NCBI database (www.ncbi.nlm.nih.gov). Protein analyses were performed using Protparam site, PROTSCALE, TMM application, PEPTIDE CUTTER, NETNGLYC and TARGETTP. The protein model and structure of MMP-9 were evaluated using SWISSMODEL. Results: Based on the study, it showed that MMP-9 is located on 20q13.12. It is involved in extracellular matrix breakdown, and this enzyme degrades type IV and V collagens. Based on the instability index (II), the protein was found to be unstable. The hydrophobicity range of the MMP-9 protein was 0–7654. Among the 20 amino acids analyzed, the hydrophobicity of arginine was -4.500, while isoleucine was 4.500. Transmembrane helix analysis indicated the MMP-9 protein isoform is predominantly located outside of the cell. The predicted N-glycosylation site was at the 28th amino acid. The structural model analysis indicated that the protein model was of good quality. Conclusion: Biomolecular and bioinformatics characterization of salivary MMP-9 demonstrates strong potential as an oral cancer biomarker. The biomolecular and bioinformatics characteristics identified in this study support the potential utility of MMP-9 as an oral cancer biomarker and provide a foundation for future studies investigating its therapeutic relevance.]]>
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