Sandbox 645: Difference between revisions

Line 40:

*HIV Drugs:

1) Saquinavir (Invirase) is known to be one of the first FDA approved protease inhibitor for HIV treatment. This usually occurs by HIV protease binding an active site <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_tunnel/1'> tunnel tightly </scene>, which will prevent polyproteins from also binding. Saquniavir's chemical structure has the ability to <scene name='User:David_Canner/Sandbox_HIV/Hiv_morph2/9'> mimic the tetrahedral </scene> intermediate of the hydrolytic reaction to interact <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_cat/3'> strongly with the catalytic Asp residues</scene> <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_cat/3'> </scene>.[[Image:Saquin1.gif|frame|left|Saquinavir mesylate is a white to off-white, very fine powder with an aqueous solubility of 2.22 mg/mL at 25°C.]] Knowing that, Saquinavir is an uncleavable ligand by studying its similar conformational changes in binding saquinavir or a polypeptide. <ref>PMID: 20426757</ref> Two types of mutants can result as a way of depleting the effectiveness of the <scene name='User:David_Canner/Sandbox_HIV/Saquinavir/4'>Saquinavir</scene> ([[Invirase]]) drug. These mutants are G48V and G48V/L90M. They cause 13.5 and 149 fold reductions, respectively. Based on some quantum mechanical and molecular mechanical analysis of the interaction of the saquinavir interaction; a disturbance of the saquinavir with the mutant with a flap residue 48 leads to a change in the hydrogen bonding. This mutation leads to the loss in the inhibitor/ enzyme binding.

1) Saquinavir (Invirase) is known to be one of the first FDA approved protease inhibitor for HIV treatment. This usually occurs by HIV protease binding an active site <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_tunnel/1'> tunnel tightly </scene>, which will prevent polyproteins from also binding. Saquniavir's chemical structure has the ability to <scene name='User:David_Canner/Sandbox_HIV/Hiv_morph2/9'> mimic the tetrahedral </scene> intermediate of the hydrolytic reaction to interact <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_cat/3'> strongly with the catalytic Asp residues</scene> <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_cat/3'> </scene>.

[[Image:Saquin1.gif|frame|left|Saquinavir mesylate is a white to off-white, very fine powder with an aqueous solubility of 2.22 mg/mL at 25°C.]]

Knowing that, Saquinavir is an uncleavable ligand by studying its similar conformational changes in binding saquinavir or a polypeptide. <ref>PMID: 20426757</ref> Two types of mutants can result as a way of depleting the effectiveness of the <scene name='User:David_Canner/Sandbox_HIV/Saquinavir/4'>Saquinavir</scene> ([[Invirase]]) drug. These mutants are G48V and G48V/L90M. They cause 13.5 and 149 fold reductions, respectively. Based on some quantum mechanical and molecular mechanical analysis of the interaction of the saquinavir interaction; a disturbance of the saquinavir with the mutant with a flap residue 48 leads to a change in the hydrogen bonding. This mutation leads to the loss in the inhibitor/ enzyme binding.

Sandbox 645: Difference between revisions

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@@ Line 40: / Line 40: @@
 *HIV Drugs:
-)	Saquinavir (Invirase) is known to be one of the first FDA approved protease inhibitor for HIV treatment. This usually occurs by HIV protease binding an active site <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_tunnel/1'> tunnel tightly </scene>, which will prevent polyproteins from also binding.  Saquniavir's chemical structure has the ability to <scene name='User:David_Canner/Sandbox_HIV/Hiv_morph2/9'> mimic the tetrahedral </scene>  intermediate of the hydrolytic reaction to interact <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_cat/3'> strongly with the catalytic Asp residues</scene> <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_cat/3'> </scene>.[[Image:Saquin1.gif|frame|left|Saquinavir mesylate is a white to off-white, very fine powder with an aqueous solubility of 2.22 mg/mL at 25°C.]] Knowing that, Saquinavir is an uncleavable ligand by studying its similar conformational changes in binding saquinavir or a polypeptide. <ref>PMID: 20426757</ref> Two types of mutants can result as a way of depleting the effectiveness of the <scene name='User:David_Canner/Sandbox_HIV/Saquinavir/4'>Saquinavir</scene> ([[Invirase]]) drug. These mutants are G48V and G48V/L90M. They cause 13.5 and 149 fold reductions, respectively. Based on some quantum mechanical and molecular mechanical analysis of the interaction of the saquinavir interaction; a disturbance of the saquinavir with the mutant with a flap residue 48 leads to a change in the hydrogen bonding. This mutation leads to the loss in the inhibitor/ enzyme binding.
+)	Saquinavir (Invirase) is known to be one of the first FDA approved protease inhibitor for HIV treatment. This usually occurs by HIV protease binding an active site <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_tunnel/1'> tunnel tightly </scene>, which will prevent polyproteins from also binding.  Saquniavir's chemical structure has the ability to <scene name='User:David_Canner/Sandbox_HIV/Hiv_morph2/9'> mimic the tetrahedral </scene>  intermediate of the hydrolytic reaction to interact <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_cat/3'> strongly with the catalytic Asp residues</scene> <scene name='User:David_Canner/Sandbox_HIV/Saquinavir_cat/3'> </scene>.
+[[Image:Saquin1.gif|frame|left|Saquinavir mesylate is a white to off-white, very fine powder with an aqueous solubility of 2.22 mg/mL at 25°C.]]
+Knowing that, Saquinavir is an uncleavable ligand by studying its similar conformational changes in binding saquinavir or a polypeptide. <ref>PMID: 20426757</ref> Two types of mutants can result as a way of depleting the effectiveness of the <scene name='User:David_Canner/Sandbox_HIV/Saquinavir/4'>Saquinavir</scene> ([[Invirase]]) drug. These mutants are G48V and G48V/L90M. They cause 13.5 and 149 fold reductions, respectively. Based on some quantum mechanical and molecular mechanical analysis of the interaction of the saquinavir interaction; a disturbance of the saquinavir with the mutant with a flap residue 48 leads to a change in the hydrogen bonding. This mutation leads to the loss in the inhibitor/ enzyme binding.