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Access type: UnknownAuthor: search.filters.author.Jitonnom, Jitrayut

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    Item type:Publication,
    3D-QSAR studies of 4-aminoquinoline-pyrimidine hybrids as antimalarial inhibitors targeting wild-type P. falciparum dihydrofolate reductase
    (2025-11-01)
    Jitonnom, Jitrayut
    ;
    Jitonnom, Wijitra
    ;
    Tue-Ngeun, Panthip
    ;
    Saparpakorn, Patchreenart
    ;
    Hannongbua, Supa
    Three-dimensional quantitative structure–activity relationship (3D-QSAR) was determined on a set of 4-aminoquinoline-pyrimidine hybrids to elucidate the 3D structural features affecting the antimalaria activity against wild-type Plasmodium falciparum dihydrofolate reductase (PfDHFR). Several combined analyses of comparative molecular field (CoMFA), comparative molecular similarity indices (CoMSIA) and noncovalent interaction (NCI) were carried out. The 3D descriptors capturing steric, electrostatic and hydrophobic features of molecules and their correlation with experimental activity were established (CoMFA; q<sup>2</sup>= 0.506, r<sup>2</sup>= 0.875, SEE = 0.227 and CoMSIA; q<sup>2</sup>= 0.614, r<sup>2</sup>= 0.871, SEE = 0.230). Key structural features are drawn from the models: The R<sup>1</sup>substituent prefers small, less steric groups, while the R<sup>2</sup>substituent favors larger, more sterically bulky hydrophobic groups. Introducing hydrogen bond acceptor and donor groups at R<sup>2</sup>and the N-substituted linkage enhances activity. The docking and NCI results revealed extensive hydrophobic interactions and its stabilization to the binding process of PfDHFR.
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    3D-QSAR and molecular docking studies of peptide-hybrids as dengue virus NS2B/NS3 protease inhibitors
    (2024-06-01)
    Jitonnom, Jitrayut
    ;
    Meelua, Wijitra
    ;
    Tue-nguen, Panthip
    ;
    Saparpakorn, Patchreenart
    ;
    Hannongbua, Supa
    Global warming and climate change have made dengue disease a global health issue. More than 50 % of the world's population is at danger of dengue virus (DENV) infection, according to the World Health Organization (WHO). Therefore, a clinically approved dengue fever vaccination and effective treatment are needed. Peptide medication development is new pharmaceutical research. Here we intend to recognize the structural features inhibiting the DENV NS2B/NS3 serine protease for a series of peptide-hybrid inhibitors (R<inf>1</inf>–R<inf>2</inf>-Lys-R<inf>3</inf>-NH<inf>2</inf>) by the 3D-QSAR technique. Comparative molecular field analysis (q<sup>2</sup> = 0.613, r<sup>2</sup> = 0.938, r<sup>2</sup><inf>pred</inf> = 0.820) and comparative molecular similarity indices analysis (q<sup>2</sup> = 0.640, r<sup>2</sup> = 0.928, r<sup>2</sup><inf>pred</inf> = 0.693) were established, revealing minor, electropositive, H-bond acceptor groups at the R<inf>1</inf> position, minor, electropositive, H-bond donor groups at the R<inf>2</inf> position, and bulky, hydrophobic groups at the R<inf>3</inf> position for higher inhibitory activity. Docking studies revealed extensive H-bond and hydrophobic interactions in the binding of tripeptide analogues to the NS2B/NS3 protease. This study provides an insight into the key structural features for the design of peptide-based inhibitors of DENV NS2B/NS3 protease.