<p>In this research, structure of SARS-CoV-2
spike glycoprotein S1 and S2 along with TMPRSS2, TMPRSS4, TMPRSS11A, TMPRSS11D
and TMPRSS11E serine protease (which activates S1 and S2) are used for docking
with repurposed inhibitor drug molecules. We searched for a universally active
drug molecule which binds with glycoproteins and serine protease with binding
energy above a pre-set threshold value, thus single handedly inhibits the virus
glycoprotein interaction with ACE-II receptor on human cell preventing the virus
RNA transfer to human cell. Through data analysis performed on binding energies
of the selected repurposed inhibitors, we found out five molecules to have high
binding energies on both spike glycoproteins and serine protease, while showing
less variance in their binding energies. Among these five, Edoxaban is an
FDA approved commercially available drug molecule. Hence, high binding molecular
inhibitors for spike glycoprotein and serine protease for treatment of
SARS-CoV-2 were identified. </p>
<p>In this research we used the structure of SARS-CoV-2
related, recently mapped, atomic
structure of nsp10/16 proteins for docking with some known drug molecular
structures at pH 7 and 5. Chosen
molecules were azo -N=N- and -COOH derivatives. It was revealed that the molecules
showed good binding energy with nsp10/16
protein at both pH. These molecules can act as protein-nucleic acid
interface (PNAI) inhibitor drug molecules. Such molecules can be used in
combination with polymerase and protease inhibitors for treatment of SARS-CoV-2.
</p>
<p>In this research we used the structure of
SARS-CoV-2 main protease (Mpro) for docking with Anti-HIV protease inhibitor drug molecules within pH 4-8. By carrying
out the variance analysis of binding energies at pH 4-8, it was revealed that the
binding energy and mode of interaction of the potential ligands with
SARS-CoV-2 Mpro, was dependent on variation of pH. We found out that two of the
selected protease inhibitors have differential binding characteristics with
changing pH hence their binding energies and mode of interaction depends upon
intracellular pH. This differential
binding behavior can lead to development of pH selective potent drug molecules
for binding with viral protease at lowered intracellular pH of virus infected
cell. </p>
<p>In this research we used the structure of SARS-CoV-2
related, recently mapped, atomic
structure of nsp10/16 proteins for docking with some known drug molecular
structures at pH 7 and 5. Chosen
molecules were azo -N=N- and -COOH derivatives. It was revealed that the molecules
showed good binding energy with nsp10/16
protein at both pH. These molecules can act as protein-nucleic acid
interface (PNAI) inhibitor drug molecules. Such molecules can be used in
combination with polymerase and protease inhibitors for treatment of SARS-CoV-2.
</p>
Two novel 1,2-diol containing azo dyes have been synthesized for application on polymeric textile substrates. We used multistep synthesis scheme which involved selectively bonding azo chromophore with glycerol moiety such that only one alcohol out of the three gets bonded to the chromophore while rest two remain unchanged. The 1,2-diol moiety, common in both dyes, is responsible for forming hydrogen bonds with polar sites on a polymeric substrate. The molecular structure of the final molecule and synthesized intermediates were elucidated by UV/Vis, FT-IR, MS (EI, ESI, and CI) and 1 H-NMR spectroscopic techniques. Dyes were applied to polyester and nylon 66 fabrics as disperse dyes by exhaust dyeing method and furnished good to excellent fastness properties on both of them.
<p class="Abstract">Four new bioactive aryl triester derivatives of glycerol and benzoic acids were synthesized. The synthetic compounds were studied for their antimicrobial and urease inhibition activities. Esterification was carried out by using carbonyldiimidazole to enhance the acyl elimination addition reaction with benzoic acid derivatives. The structure of triglycerides were studied by EI-MS, <sup>1</sup>H, <sup>13</sup>C-NMR, FT-IR and elemental analysis. All synthetic compounds showed urease inhibition activity with highest value of IC<sub>50 </sub>value 22.4 ± 0.45 μM which is nearest to standard thiourea IC<sub>50 </sub>value (21.6 ± 0.12 μM). Except compound (3d), all other compounds exhibited antimicrobial activity against <em>Streptococcus pneumoniae, Staphylococcus epidermidis, Bacillus pumilus, Escherichia coli, Pseudomonas aeruginosa</em> and <em>Candida albican</em>.</p><p><strong>Video Clip of Methodology:</strong></p><p>7 min 59 sec <a href="https://youtube.com/v/PvGTYUxO7-4">Full Screen</a> <a href="https://youtube.com/watch?v=PvGTYUxO7-4">Alternate</a> </p>
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