Abstract
We report the interaction between a well-known antibiotic chloramphenicol (Clp) and the protein, bovine pancreatic trypsin. Both steady-state and time-resolved measurements, along with binding constant measurements which varies inversely with temperature, emphasize the static quenching mechanism induced by the added Clp. Additionally, Isothermal Titration Calorimetry (ITC) and docking analyses conclusively substantiate the role of hydrophobic interactions as the primary mode of binding. The structural alteration of trypsin in presence of Clp was monitored by Circular Dichroism (CD) spectroscopy. Addition of strong electrolytes enhances the binding affinity of Clp with trypsin which also increases hydrophobic interaction, due to salting out effect.
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