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Title |
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An in silico approach to map the binding site of doxorubicin on hemoglobin
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Authors |
Shahper Nazeer Khan1 and Asad Ullah Khan1, 2, *
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Affiliation |
1Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh-202002, India; 2Bioinformatics distributed Information sub-centre, AMU, Aligarh-202002, India
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91 571 2723088
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91 571 2721776; * Corresponding author
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Article Type |
Hypothesis
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Date |
received March 08, 2008; revised April 18, 2008; accepted April 22, 2008; published July 14, 2008
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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.
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Keywords |
hemoglobin; doxorubicin; molecular docking; binding site | |
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Citation |
Khan and Khan, Bioinformation 2(9): 401-404 (2008)
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Edited by |
V. S. Mathura
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ISSN |
0973-2063
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Publisher |
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License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |