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Title |
Molecular modeling and prediction of binding mode and relative binding affinity of Art-Qui-OH with P. falciparum Histo-Aspartic Protease (HAP) |
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Authors |
Rajani Kanta Mahapatra1, 2*, Niranjan Behera1 & Pradeep Kumar Naik3 |
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Affiliation |
1School of Life Sciences, Sambalpur University, Burla, Odisha-768019, India; 2School of Biotechnology, KIIT University, Bhubaneswar, Odisha-751024, India; 3Department of Biotechnology & Bioinformatics, JUIT, Solan, Himachal Pradesh-173 215, India.
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rmohapatra@kiitbiotech.ac.in; *Corresponding author
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Article Type |
Hypothesis
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Date |
Received August 15, 2012; Accepted August 20, 2012; Published September 11, 2012 |
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Abstract |
The relative binding affinity in terms of ??G bind-cald value of the antimalarial compound artemisinin-quinine hybrid is primarily derived and is discussed in this article with reference to the ?G bind-cald values of two known inhibitors Pepstatin-A and KNI-10006 complexed with HAP enzyme. The ?G bind-cald value for KNI-10006 and Pepstatin-A is -14.10 kcal/mol and -13.09 kcal/mol respectively. The MM-GB/SA scoring results in the relative binding energy (??G bind-cald) of the hybrid molecule with respect to Pepstatin-A as 2.43 kcal/mol and 3.44 kcal/mol against KNI-10006. The overall binding mode of Art-Qui-OH resembles that of Pepstatin-A binding in HAP active site. We suggest here that the ??G bind-cald value & proposed binding mode of the Art-Qui-OH for HAP enzyme should be considered for further structure-based drug design effort.
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Keywords |
HAP, Art-Qui-OH, ??G bind-cald, ?G score
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Citation |
Mahapatra et al.
Bioinformation 8(17): 827-833 (2012) |
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Edited by |
P Kangueane
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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. |