Sandbox 9888: Difference between revisions

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Remicade (Infliximab) is a chimeric IgG1 monoclonal antibody consisting of 597 amino acids, weighing 149,000 Daltons <ref>PMID:23504311</ref>. This chimeric monoclonal antibody is produced when the variable regions of a murine antibody (25%) is fused with the constant regions of a human antibody (75%) at the hinge region through a genetic engineering process <ref>PMID:17592358</ref>. Within the hinge region, intramolecular disulfide bonds stabilize the two fragment antigen binding regions (Fab) to the fragment crystallizable region (Fc). <scene name='74/744162/Variable_chains_hc/1'>Click here to view separated Fab and Fc regions</scene>. The Fab regions are comprised of both a heavy and light chain, while the Fc region consist of only a heavy chain. Located in the folded Vh and Ch domains of the heavy chain, amino acid residues Glu-1 to Thr-226 are found <ref>PMID:23504311</ref>. <scene name='74/744162/Heavy_chain/1'>The heavy chain region is highlighted here, and only (1 of 3) molecules are shown, for simplicity</scene>. In addition, the <scene name='74/744162/Light_chain/1'>light chain</scene> is composed of residues Asp-1 to Cys-214 that fold into the Vl and Cl domain <ref>PMID:23504311</ref>. The heavy and light chain at the N-terminus form the variable region that functions as a receptor binding site.

After intravenously injecting Infliximab, the p55 and p75 receptors (TNF-R?) on TNF-α are neutralized when bound to the drugs high affinity receptor binding sites <ref> PMID: 17916444 </ref>. The complex formed is stabilized through the vast array of weak interactions between the two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces <ref>PMID:23504311</ref>. Specifically, TNF-α contributes to the stability by creating a hydrophobic interface <ref>PMID:2777790</ref> through amino acid residues such as the <scene name='74/744162/Tyr_141_atom/1'>Tyr-141 side chain</scene> <ref>PMID:23504311</ref>. This interface is formed primarily by the C-D and E-F <scene name='74/744162/Loops_tnf/2'>loop residues</scene> connecting the antiparallel 8-stranded Beta sheets <ref>PMID:23504311</ref>. To view the loop residues of the full structure complex, <scene name='74/744162/Loops_tnf_3molecule/1'>click here</scene>. These favorable interactions are essential to the complex formed between TNF-α and infliximab Fab.

After intravenously injecting Infliximab, the p55 and p75 receptors (TNF-R?) on TNF-α are neutralized when bound to the drugs high affinity receptor binding sites <ref> PMID: 17916444 </ref>. The complex formed is stabilized through the vast array of weak interactions between the two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces <ref>PMID:23504311</ref>. Specifically, TNF-α contributes to the stability by creating a <scene name='74/744162/Hydrophobic_interface/1'>hydrophobic interface</scene> <ref>PMID:2777790</ref> through amino acid residues such as the <scene name='74/744162/Tyr_141_atom/3'>Tyr-141 side chain</scene> <ref>PMID:23504311</ref>. This interface is formed primarily by the C-D and E-F <scene name='74/744162/Loops_tnf/2'>loop residues</scene> connecting the antiparallel 8-stranded Beta sheets <ref>PMID:23504311</ref>. To view the loop residues of the full structure complex, <scene name='74/744162/Loops_tnf_3molecule/1'>click here</scene>. These favorable interactions are essential to the complex formed between TNF-α and infliximab Fab.

== History of Remicade ==

Sandbox 9888: Difference between revisions

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 Remicade (Infliximab) is a chimeric IgG1 monoclonal antibody consisting of 597 amino acids, weighing 149,000 Daltons <ref>PMID:23504311</ref>. This chimeric monoclonal antibody is produced when the variable regions of a murine antibody (25%)  is fused with the constant regions of a human antibody (75%) at the hinge region through a genetic engineering process <ref>PMID:17592358</ref>. Within the hinge region, intramolecular disulfide bonds stabilize the two fragment antigen binding regions (Fab) to the fragment crystallizable region (Fc). <scene name='74/744162/Variable_chains_hc/1'>Click here to view separated Fab and Fc regions</scene>. The Fab regions are comprised of both a heavy and light chain, while the Fc region consist of only a heavy chain. Located in the folded Vh and Ch domains of the heavy chain, amino acid residues Glu-1 to Thr-226 are found <ref>PMID:23504311</ref>. <scene name='74/744162/Heavy_chain/1'>The heavy chain region is highlighted here, and only (1 of 3) molecules are shown, for simplicity</scene>. In addition, the <scene name='74/744162/Light_chain/1'>light chain</scene> is composed of residues Asp-1 to Cys-214 that fold into the Vl and Cl domain <ref>PMID:23504311</ref>. The heavy and light chain at the N-terminus form the variable region that functions as a receptor binding site.
-After intravenously injecting Infliximab, the p55 and p75 receptors (TNF-R?) on TNF-α are neutralized when bound to the drugs high affinity receptor binding sites <ref> PMID: 17916444 </ref>. The complex formed is stabilized through the vast array of weak interactions between the two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces <ref>PMID:23504311</ref>. Specifically, TNF-α contributes to the stability by creating a hydrophobic interface <ref>PMID:2777790</ref> through amino acid residues such as the <scene name='74/744162/Tyr_141_atom/1'>Tyr-141 side chain</scene> <ref>PMID:23504311</ref>. This interface is formed primarily by the C-D and E-F <scene name='74/744162/Loops_tnf/2'>loop residues</scene> connecting the antiparallel 8-stranded Beta sheets <ref>PMID:23504311</ref>. To view the loop residues of the full structure complex, <scene name='74/744162/Loops_tnf_3molecule/1'>click here</scene>. These favorable interactions are essential to the complex formed between TNF-α and infliximab Fab.
+After intravenously injecting Infliximab, the p55 and p75 receptors (TNF-R?) on TNF-α are neutralized when bound to the drugs high affinity receptor binding sites <ref> PMID: 17916444 </ref>. The complex formed is stabilized through the vast array of weak interactions between the two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces <ref>PMID:23504311</ref>. Specifically, TNF-α contributes to the stability by creating a <scene name='74/744162/Hydrophobic_interface/1'>hydrophobic interface</scene> <ref>PMID:2777790</ref> through amino acid residues such as the <scene name='74/744162/Tyr_141_atom/3'>Tyr-141 side chain</scene> <ref>PMID:23504311</ref>. This interface is formed primarily by the C-D and E-F <scene name='74/744162/Loops_tnf/2'>loop residues</scene> connecting the antiparallel 8-stranded Beta sheets <ref>PMID:23504311</ref>. To view the loop residues of the full structure complex, <scene name='74/744162/Loops_tnf_3molecule/1'>click here</scene>. These favorable interactions are essential to the complex formed between TNF-α and infliximab Fab.
 == History of Remicade ==