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Objective: S100 proteins, the low molecular weight calcium binding proteins, have ‘EF hand’ type conformation. They are identified as markers for various diseases. A member of S100 protein family, S100A9 is involved, in performing important biological functions, by coordinating with S100A8. S100A9 targeted interactions of quinoline-3carboxamides, differentiates quinoline derivative interaction among varying single point substituents. Inhibition of protein interaction with many important biological markers as RAGE, TLR4/MD2 and others, was accomplished by quinoline-3-carboxamides. Methods: Two quinoline derivatives identified from Toddalia aculeata are analysed for their molecular and ligand properties. Results: Toxicity analysis, show ADMET properties of phytoquinolines, to be supportive. Molecular binding with S100A9 and its heteromer formed with S100A8, are found analogous to binding, with substituted quinoline-3carboxamides.Among the various ligands used, a phytoquinoline derivative, and methyl substituted quinoline-3-carboxamide, show most stable interactions. Conclusion: This study proposes the use of compounds from source, as potential ligands to target marker S100A9 and its heterodimer.

Calprotectin Complex Interactions with Phytoquinolines and New Target Binding Alternates Calprotectin complex and Phytoquinolines