673475-85-9Relevant academic research and scientific papers
Antimalarial activity of HIV-1 protease inhibitor in chromone series
Lerdsirisuk, Pradith,Maicheen, Chirattikan,Ungwitayatorn, Jiraporn
, p. 142 - 147 (2014)
Increasing parasite resistance to nearly all available antimalarial drugs becomes a serious problem to human health and necessitates the need to continue the search for new effective drugs. Recent studies have shown that clinically utilized HIV-1 protease (HIV-1 PR) inhibitors can inhibit the in vitro and in vivo growth of Plasmodium falciparum. In this study, a series of chromone derivatives possessing HIV-1 PR inhibitory activity has been tested for antimalarial activity against P. falciparum (K1 multi-drug resistant strain). Chromone 15, the potent HIV-1 PR inhibitor (IC50 = 0.65 μM), was found to be the most potent antimalarial compound with IC50 = 0.95 μM while primaquine and tafenoquine showed IC50 = 2.41 and 1.95 μM, respectively. Molecular docking study of chromone compounds against plasmepsin II, an aspartic protease enzyme important in hemoglobin degradation, revealed that chromone 15 exhibited the higher binding affinity (binding energy = -13.24 kcal/mol) than the known PM II inhibitors. Thus, HIV-1 PR inhibitor in chromone series has the potential to be a new class of antimalarial agent.
Biological activity evaluation and molecular docking study of chromone derivatives as cyclooxygenase-2 inhibitors
Maicheen, Chirattikan,Phosrithong, Narumol,Ungwitayatorn, Jiraporn
, p. 662 - 671 (2017/02/15)
A series of chromone derivatives have been evaluated as potential cyclooxygenase-2 (COX-2) inhibitors. The four most potent compounds, 48, 41, 39, and 35 displayed IC50 values of 3.30, 6.86, 7.36 and 7.46 μM, respectively. Compounds 35 and 38 showed higher selectivity for COX-2 (selectivity index, SI = 7.48 and 5.46, respectively) than celecoxib (SI = 4.17 in the same test) whereas compound 39 showed comparable selectivity (SI = 4.19) to celecoxib. The molecular volumes of compounds 35 (312.84 ?3) and 38 (314.18 ?3) were similar to celecoxib (299.28 ?3) but larger than ibuprofen (211.83 ?3). Docking results were in good agreement with the experimental biological data in terms of evaluation of binding energy and binding mode. Compounds 35, 38, and 39 had higher binding affinity against COX-2 (binding energy between ?9.77 and ?11.42 kcal/mole) than COX-1 (binding energy between ?6.28 and ?7.88 kcal/mole). These three chromone compounds also displayed active conformation in the same orientation as that of celecoxib. Thus, compounds in this series has the potential to be a new class of selective COX-2 inhibitor.
Synthesis, in vitro evaluation, and docking studies of novel chromone derivatives as HIV-1 protease inhibitor
Ungwitayatorn, Jiraporn,Wiwat, Chanpen,Samee, Weerasak,Nunthanavanit, Patcharawee,Phosrithong, Narumol
experimental part, p. 152 - 161 (2011/10/03)
Novel chromone derivatives with a benzopyran-4-one scaffold have been prepared by the one-pot cyclization reaction. The in vitro inhibitory activity of these new compounds towards HIV-1 protease have been evaluated using stop time HPLC method as the preliminary screening. The most potent compound, 7,8-dihydroxy-2-(3′-trifluoromethyl phenyl)-3-(3″- trifluoromethylbenzoyl)chromone (32), showed IC50 = 0.34 μM. The molecular docking study supported results from experimental activity testing and also provided structure-activity relationship of this series.
