@article {2208,
	title = {Unveiling Potential Therapies: Molecular Docking Analysis of CAMKK2 and Its Mutant Variants with CAMKK2 Inhibitors in Indonesian Patients with HIV-Sensory Neuropathy},
	journal = {Pharmacognosy Journal},
	volume = {16},
	year = {2024},
	month = {February 2024},
	pages = {46-51},
	type = {Original Article},
	chapter = {46},
	abstract = {<p class="rtejustify">HIV sensory neuropathy (HIV-SN) is one among many complications that impair patients{\textquoteright} quality of life. Studies in Asian and African populations found that single nucleotide polymorphisms (SNPs) of calcium/ calmodulin-dependent protein kinase 2 (CAMKK2) influence the risk of HIV-SN. This study attempts to explain the influence of CAMKK2 mutations on HIV SN by studying bioinformatics interactions between CAMKK2, its mutants, and their inhibitors by molecular docking with AutoDock in order to observe their interactions with CAMKK2 inhibitors. Results showed that CAMKK2{\textquoteright}s binding energy with its native ligand (ATP) is stronger than the mutant variant of CAMKK2MT85 and CAMKK2MT363. Conversely, interaction between CAMKK2 and its inhibitors (KN-93, STO-609, and trifluoperazine) have the lowest mean binding energy compared to CAMKK2MT85 and CAMKK2MT363. This indicates that the mutant variants have weaker interactions with the native ligand and the inhibitors, therefore disrupting the normal function of CAMKK2, its interactions with the inhibitors, while increasing the likelihood of HIV-SN.</p>
},
	keywords = {CAMKK2 inhibitors, HIV-SN, Molecular docking, mutation, SNP},
	doi = {10.5530/pj.2024.16.7},
	author = {Ahmad Yanuar Safri and Salim Harris and Putera Dewa Haryono and Ariane Benina Budiwan and Eugenia Isadora and Aisyah Fitriannisa Prawiningrum and Fadilah Fadilah}
}
@article {1917,
	title = {Prediction of MMP-9 Polymorphism Impacts on MDR-TB by Molecular Simulation and Network Interaction},
	journal = {Pharmacognosy Journal},
	volume = {14},
	year = {2022},
	month = {December 2022},
	pages = {833-841},
	type = {Research Article },
	chapter = {833},
	abstract = {<p class="rtejustify">MMP-9 overexpression is associated with a poor outcome in MDR-TB patients, indicating that MMP-9 is a suitable target for MDR-TB therapy. MMP-9 also includes SNPs that occur at inhibitor binding areas as well as zinc ions. As a result of polymorphisms, the usage of MMP-9 inhibitors for MDR-TB might vary. Through molecular simulation, it has been found that the mutant MMP-9 has a larger cavity and a more lipophilic surface. The docking tests revealed that EGTA had the least amount of binding energy to both wild-type and mutant MMP-9. The wildtype MMP-9 can bind zinc when EGTA is in the active site. This shows that using EGTA to chelate Zn is only partially successful. However, the binding energy of EGTA at the active site suggests that it may be a competitor to MMP-9 substrates. On the other hand, Zn is not involved in the interaction of the mutant MMP-9-EGTA complex.</p>
},
	keywords = {Gene polymorphism, Matrix metalloproteinase 9, Molecular simulation., Multidrug resistant TB},
	doi = {10.5530/pj.2022.14.176},
	author = {Anse Diana Valentiene Messah and Sawitri Darmiati and Cleopas Marthin Rumende and Retno Ariza Soemarwoto and Joedo Prihartono and Asmarinah and Fadilah Fadilah and Aisyah Fitriannisa Prawiningrum}
}
