Outer membrane protein 100 of Aggregatibacter actinomycetemcomitans act as a biopharmaceutical target for photodynamic therapy: An in silico analysis

Abstract

BackgroundPeriodontitis is a polymicrobial, chronic, and degenerative disease that can lead to destruction of the teeth-supporting tissues and eventually to loss of teeth. Aggregatibacter actinomycetemcomitans is predominantly associated with periodontal diseases. Outer membrane protein (Omp) 100 is a more important virulence factor of A. actinomycetemcomitans due to the effect of adhesion and invasion into human gingival epithelial cells. Attachment of A. actinomycetemcomitans inhibition is significant in the treatment process. MethodsWe evaluated the capacity of Omp100 in A. actinomycetemcomitans as a novel target for photodynamic therapy (PDT) using a range of bioinformatic tools. In silico analysis was used to predict molecular modeling, the hierarchical nature of protein structure and backbone, and sub-cellular localization. ResultsThe results showed that Omp100 is most similar to thiamine-phosphate pyrophosphorylase [Haemophilus influenzae PittGG], with a 74% similarity. The predicted structure of Omp100 displayed that it is a protein with positive charge (10.4) in pH 7 and alpha helix dominates other secondary structures located outside the cell. Protein-protein interaction network showed that Omp100 interacted with extracellular matrix protein adhesion, glycoside hydrolase, Omp 64, phospholipase D/Transphosphatidylase, Flp pilus assembly protein, and heme acquisition system receptor. ConclusionAccording to the results, anionic indocyanine green tends to interact with Omp100 during PDT as a major target.