Abstract
Colchicine (Col), a naturally occurring alkaloid, has been used as an anti-inflammatory, anti-fibrotic, and anti-tumor drug. The present study reports in vitro interaction between Col and hen egg white lysozyme (HEWL) by spectroscopy, isothermal titration calorimetry (ITC), and molecular docking techniques. The fluorescence results indicated that Col quenches the intrinsic fluorescence of HEWL through static quenching mechanism which is also substantiated by UV–visible spectroscopy. The average distance (r) between donor (HEWL) and acceptor (Col) was evaluated by Forster’s resonance energy transfer theory. Thermodynamic parameters obtained from ITC suggested that hydrophobic interaction plays a major role in the complex formation, and it is an entropically driven process. Col altered the secondary structure of HEWL revealed by circular dichroism which is further corroborated by synchronous, 3D fluorescence and FTIR techniques. In addition, molecular docking was employed to find out binding site of Col on HEWL and amino acid residues involved in the binding process. This study is expected to provide insights into the type of interaction and binding mechanism of Col with HEWL.
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 callDisclaimer: 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.
