scholarly journals Interaction between Gallotannin and a Recombinant Form of Arginine Kinase of Trypanosoma brucei: Thermodynamic and Spectrofluorimetric Evaluation

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
O. S. Adeyemi ◽  
A. F. Sulaiman ◽  
O. M. Iniaghe
Keyword(s):  
Enzyme Activity ◽  
Molecular Docking ◽  
Trypanosoma Brucei ◽  
Arginine Kinase ◽  
Docking Studies ◽  
Recombinant Form ◽  
Binding Properties ◽  
Mechanism Of Inhibition ◽  
Static Data ◽  
Inhibitory Interactions

Current chemotherapies against trypanosomiasis are beset with diverse challenges, a situation which underscores the numerous research efforts aimed at finding newer and effective treatments. Arginine kinase of trypanosome has been validated as target for drug development against trypanosomiasis. The present study investigated the interaction between a recombinant form of the arginine kinase (rTbAK) of trypanosome and gallotannin. The interaction between gallotannin and recombinant arginine kinase of Trypanosoma brucei caused significant decrease of enzyme activity. Kinetic analysis revealed the interaction to be of noncompetitive inhibition. Further thermodynamic analysis showed that the interaction between gallotannin and the recombinant arginine kinase was nonspontaneous and involved hydrophobic forces. The Ksv values and the FRET analysis suggest that static quenching of fluorescence intensity by gallotannin was static. Data revealed inhibitory interactions between gallotannin and rTbAK of trypanosome. Although the mechanism of inhibition is not clear yet, molecular docking studies are ongoing to clearly define the inhibitory interactions between the gallotannin and rTbAK. The knowledge of such binding properties would enrich development of selective inhibitors for the arginine kinase of Trypanosoma brucei.

scholarly journals Apoferritin and Apoferritin-Capped Metal Nanoparticles Inhibit Arginine Kinase of Trypanosoma brucei

Molecules ◽  
2020 ◽  
Vol 25 (15) ◽  
pp. 3432
Author(s):  
Oluyomi Stephen Adeyemi ◽  
Afolake T. Arowolo ◽  
Helal F. Hetta ◽  
Salim Al-Rejaie ◽  
Damilare Rotimi ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Metal Nanoparticles ◽  
Kinetic Parameters ◽  
Trypanosoma Brucei ◽  
Kinase Activity ◽  
Arginine Kinase ◽  
Inhibition Constant ◽  
Binding Properties ◽  
Inhibitory Potential ◽  
Relative Inhibition

The aim of this study was to explore the inhibitory potential of apoferritin or apoferritin-capped metal nanoparticles (silver, gold and platinum) against Trypanosomabrucei arginine kinase. The arginine kinase activity was determined in the presence and absence of apoferritin or apoferritin-capped metal nanoparticles. In addition, kinetic parameters and relative inhibition of enzyme activity were estimated. Apoferritin or apoferritin-capped metal nanoparticles’ interaction with arginine kinase of T. brucei led to a >70% reduction in the enzyme activity. Further analysis to determine kinetic parameters suggests a mixed inhibition by apoferritin or apoferritin-nanoparticles, with a decrease in Vmax. Furthermore, the Km of the enzyme increased for both ATP and L-arginine substrates. Meantime, the inhibition constant (Ki) values for the apoferritin and apoferritin-nanoparticle interaction were in the submicromolar concentration ranging between 0.062 to 0.168 nM and 0.001 to 0.057 nM, respectively, for both substrates (i.e., L-arginine and ATP). Further kinetic analyses are warranted to aid the development of these nanoparticles as selective therapeutics. Also, more studies are required to elucidate the binding properties of these nanoparticles to arginine kinase of T. brucei.

scholarly journals Design and Synthesis of N-phenyl Phthalimides as Potent Protoporphyrinogen Oxidase Inhibitors

Molecules ◽  
2019 ◽  
Vol 24 (23) ◽  
pp. 4363
Author(s):  
Wei Gao ◽  
Xiaotian Li ◽  
Da Ren ◽  
Susu Sun ◽  
Jingqian Huo ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Enzyme Activity ◽  
Molecular Docking ◽  
Molecular Design ◽  
Design Strategy ◽  
Docking Studies ◽  
Activity Assay ◽  
Enzyme Activity Assay ◽  
Protoporphyrinogen Oxidase ◽  
Design And Synthesis

Protoporphyrinogen oxidase (PPO) has been identified as one of the most promising targets for herbicide discovery. A series of novel phthalimide derivatives were designed by molecular docking studies targeting the crystal structure of mitochondrial PPO from tobacco (mtPPO, PDB: 1SEZ) by using Flumioxazin as a lead, after which the derivatives were synthesized and characterized, and their herbicidal activities were subsequently evaluated. The herbicidal bioassay results showed that compounds such as 3a (2-(4-bromo-2,6-difluorophenyl) isoindoline-1,3-dione), 3d (methyl 2-(4-chloro-1,3-dioxoisoindolin-2-yl)-5-fluorobenzoate), 3g (4-chloro-2-(5-methylisoxazol-3-yl) isoindoline-1,3-dione), 3j (4-chloro-2-(thiophen-2-ylmethyl) isoindoline-1,3-dione) and 3r (2-(4-bromo-2,6-difluorophenyl)-4-fluoroisoindoline-1,3-dione) had good herbicidal activities; among them, 3a showed excellent herbicidal efficacy against A. retroflexus and B. campestris via the small cup method and via pre-emergence and post-emergence spray treatments. The efficacy was comparable to that of the commercial herbicides Flumioxazin, Atrazine, and Chlortoluron. Further, the enzyme activity assay results suggest that the mode of action of compound 3a involves the inhibition of the PPO enzyme, and 3a showed better inhibitory activity against PPO than did Flumioxazin. These results indicate that our molecular design strategy contributes to the development of novel promising PPO inhibitors.

scholarly journals Synthesis, in vitro enzyme activity and molecular docking studies of new benzylamine-sulfonamide derivatives as selective MAO-B inhibitors

2020 ◽  
Vol 35 (1) ◽  
pp. 1422-1432 ◽  
Author(s):  
Begüm Nurpelin Sağlık ◽  
Derya Osmaniye ◽  
Ulviye Acar Çevik ◽  
Serkan Levent ◽  
Betül Kaya Çavuşoğlu ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Molecular Docking ◽  
Docking Studies ◽  
Molecular Docking Studies ◽  
Mao B

Calcium Channel Blockers: The Effect of Glutathione S‐Transferase Enzyme Activity and Molecular Docking Studies

2021 ◽  
Vol 6 (40) ◽  
pp. 11137-11143
Author(s):  
Cüneyt Türkeş ◽  
Arzu Öztürk Kesebir ◽  
Yeliz Demir ◽  
Ömer İrfan Küfrevioğlu ◽  
Şükrü Beydemir
Keyword(s):  
Enzyme Activity ◽  
Molecular Docking ◽  
Calcium Channel ◽  
Calcium Channel Blockers ◽  
Docking Studies ◽  
Channel Blockers ◽  
Glutathione S Transferase ◽  
Molecular Docking Studies
Sign in / Sign up

Export Citation Format

Share Document