Title

An in silico approach to map the binding site of doxorubicin on hemoglobin

Authors

Shahper Nazeer Khan¹ and Asad Ullah Khan^{1, 2,} *

Affiliation

¹Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh-202002, India; ²Bioinformatics distributed Information sub-centre, AMU, Aligarh-202002, India

Email

huzzi99@hotmail.com

91 571 2723088

91 571 2721776; * Corresponding author

Article Type

Hypothesis

Date

received March 08, 2008; revised April 18, 2008; accepted April 22, 2008; published July 14, 2008

Abstract

Binding modalities of doxorubicin (DOX), a widely used antineoplastic anthracyline antibiotic with hemoglobin (Hb) have been studied. The protein and the ligand were prepared using CORINA and protonated with insight II. The best conformation was sought by employing GOLDV. Molecular modeling calculations showed that DOX binds Hb to a non-classical drug binding site. The alpha subunit of Hb has been assigned to posses the binding site for DOX with a binding affinity (Ka) = 16.98 x10³ mol^-1. The interaction was found to be thermodynamically favorable (ΔG° = -66.23 KJmol^-1). The analysis of DOX binding site to Hb suggested that the types of interactions that contribute in this binding are hydrophobic contacts, hydrogen bonding and electrostatic interactions.

Keywords

hemoglobin; doxorubicin; molecular docking; binding site

Citation

Khan and Khan, Bioinformation 2(9): 401-404 (2008)

Edited by

V. S. Mathura

ISSN

0973-2063

Publisher

Biomedical Informatics

Copyright

Publisher

Copyright Transfer Agreement

The authors of published articles in Bioinformation automatically transfer the copyright to the publisher upon formal acceptance. However, the authors reserve right to use the information contained in the article for non commercial purposes.

License

This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.