Inhibitory efficiency of LS12 peptide by blocking Streptococcus mutants surface protein SpaP

Abstract

The SpAp protein, also known as SpaP or P1 adhesin, is a surface protein found in the bacterium Streptococcus mutans. S. mutans is a primary etiological agent in the development of dental caries (tooth decay). The SpA protein plays a crucial role in the adherence of S. mutans to tooth surfaces, which is a critical step in the formation of dental plaque. The SpAp protein is a high-molecular-weight adhesin that belongs to the antigen (I (Agli) family of cell surface proteins. It is composed of multiple repeated domains and has been shown to bind to various components present in saliva, as well as tooth surfaces. By attaching to these surfaces, S. mutans can colonize and form biofilms, which contribute to the initiation and progression of dental caries.  To detect the inhibitory effect of LS-12 peptide by blocking streptococcus mutans surface protein Spa.Toxinored and Peptide Ranker:Toxinpred is an in silico method, which is developed to predict and design toxic/non-toxic peptides and PeptideRanker is a server for the prediction of bioactive peptides. Peptide characteristics: structural characterisation of peptides is  done. Helical wheel diagram: Helical wheels are a standard way to predict protein sequence segments with either helical or non-helicpotential. Peptide Protein Docking: Peptide Docking is to treat the protein and the peptide input conformations as rigid and to perform exhaustive rigid-body docking  Zebra fish larvae toxicity: Zebrafish can be used to assess the toxicity of drug candidates in earty screening assays, sometimes in a high-throughput manner. Hence our peptide LS-12 is able to bind with SpaP so that it can inhibit its adhesion to tooth surface thereby reducing dental caries and it is non toxic due to which it can be further used for human and animal trials. However it needs further experimentation in human and Animal models for its application against Streptococcus mutans.