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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callSimilar Papers
More From: Chemical Physics Letters
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
