Abstract

Human serum albumin (HSA) is one of the main endogenous vehicles for biodistribution of molecules by blood plasma. Association constants and thermodynamic parameters for the interaction of HSA with doxorubicin were studied by docking. Docking study suggests that doxorubicin is able to interact with HSA by means of hydrogen bond with one arginine residue, whereas the hydroxyl group is inserted in a hydrophobic pocket. The estimated of Gibbs free energies (ΔG°) is equal to -9.1 kcal/mol for the best model. The negative values of ΔG° indicate a spontaneous process. The association constant value (Ka ≈ 8×103 L.mol−1) is favorable for its efficient biodistribution by blood plasma.

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 call

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.