title: Molecular modeling and prediction of binding mode and relative binding affinity of Art-Qui-OH with P. falciparum Histo-Aspartic Protease (HAP).
abstract: The relative binding affinity in terms of ΔΔG (bind-cald) value of the antimalarial compound artemisinin-quinine hybrid is primarily derived and is discussed in this article with reference to the ΔG (bind-cald) values of two known inhibitors Pepstatin-A and KNI-10006 complexed with HAP enzyme. The ΔG (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 (ΔΔG (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 ΔΔG (bind-cald) value & proposed binding mode of the Art-Qui-OH for HAP enzyme should be considered for further structure-based drug design effort.
authors.affiliation: School of Life Sciences, Sambalpur University, Burla, Odisha-768019, India ; School of Biotechnology, KIIT University, Bhubaneswar, Odisha-751024, India.
authors.forename: Rajani Kanta
authors.initials: RK
authors.lastname: Mahapatra
authors.forename: Niranjan
authors.initials: N
authors.lastname: Behera
authors.forename: Pradeep Kumar
authors.initials: PK
authors.lastname: Naik
keywords: Art-Qui-OH; HAP; ΔG score; ΔΔG bind-cald