STRUCTURAL ANALYSIS OF INTERACTION BETWEEN CCL2 CHEMOKINE PROTEIN WITH HEPARIN-COATED SILVER NANOPARTICLE

Abstract

This study investigates the binding of mouse CCL2 protein, a chemoattractant involved in various inflammatory and disease processes, to heparin-coated silver nanoparticles (HP AgNP). CCL2 interacts with immune cell surface receptors and develops concentration gradients along endothelial vessels by binding to glycosaminoglycans (GAGs) through the GAG binding domain. Recent developments have focused on the synthesis of different GAG coated nanoparticles for their potential anti-inflammatory, anti-coagulant, and antibacterial properties. The fluorescence quenching of intrinsic fluorophore of CCL2 on titrating the HP AgNP with dimer and monomer of mouse CCL2 indicates the reduced activity of tryptophan residues, suggesting an interaction between mouse CCL2 and HP AgNP. Additionally, the surface negativity of HP AgNP increases, supporting the binding and interaction with HP AGNP with CCL2 chemokine protein. The anisotropic study revealed the decreased movement of protein fluorophore after binding with HP AgNP supporting the other results validating the interaction between them AgNP and CCL2 chemokine. Further studies are necessary to comprehensively explore the interaction between HP AgNP and mouse CCL2. Overall, this study sheds light on the potential use of GAG-coated nanoparticles in targeting CCL2-mediated inflammation and diseases.