Papain: Difference between revisions

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==='''Cathepsin L'''===

<scene name='Papain/Cathepsin_l/2'>Cathepsin L</scene>, another inhibitor of Papain, interacts with the <scene name='Papain/Cathepsin_l_interaction_w_pap/1'>residues</scene> Gln-19, Cys-25, Gly-66, Asp-158, and Trp-177 by hydrogen bonding them (Cathepsin L is illustrated in CPK coloring while the interacting sites of Papain are also shown in CPK). In addition to hydrogen bonding, hydrophobic interactions exist to exclude water, allowing the papain enzyme and Cathepsin L to associate even closer. ~~Finally,~~ <scene name='~~Papain~~/~~Stacking_cathl~~/1'>~~Ring Stacking~~</scene> ~~between Trp-177 and the Capthespin L molecule hold them tightly together~~.<ref>PMID:~~18598021~~</ref> ~~Cathepsin L plays~~ a ~~role~~ in ~~many different diseases including malaria~~, ~~leishmaniasis~~, ~~Chagas' disease~~, ~~African trypanosomiasis, toxoplasmosis~~, and ~~amoebiasis~~. ~~Some studies show that there is a relation between cathepsins and certain cancers~~, ~~alzheimer~~'s, and ~~arthritis~~. <ref> PMID:~~20920298~~ </ref>

<scene name='Papain/Cathepsin_l/2'>Cathepsin L</scene>, another inhibitor of Papain, is an endosomal cysteine protease that is believed to have both physiological and pathophysiological effects on the human body. It has been indicated not only in cancer, rhematoid and osteo arthritis, and Alzheimer's, but its mechanism also appears similar to that of Ebola, SARS, Leishmania, malaria, Chagas' disease, African trypanosomiasis, toxoplasmosis, and amoebiasis.<ref> PMID:20920298 </ref> Understanding the mechanism of inhibition through the use of papain is therefore crucial to developing treatments for such diseases.<ref> PMID:18499453 </ref> Cathepsin L interacts with the <scene name='Papain/Cathepsin_l_interaction_w_pap/1'>residues</scene> Gln-19, Cys-25, Gly-66, Asp-158, and Trp-177 by hydrogen bonding them (Cathepsin L is illustrated in CPK coloring while the interacting sites of Papain are also shown in CPK). In addition to hydrogen bonding, hydrophobic interactions exist to exclude water, allowing the papain enzyme and Cathepsin L to associate even closer.

An interesting inhibitor for cathepsin L developed using papain as the model protease is that of <scene name='Sandbox_34/Clik148_inhibitor/2'>Clik-148</scene>.<ref> PMID:10600517 </ref> It forms a <scene name='Sandbox_34/Clik148_inhibit_cys25/1'>covalent ligand-bound cysteine protease complex</scene> with Cys-25. Five other residues are also involved in the bonding of Clik-148 to papain: Gln-19, Gly-66, Asp-158, Trp-177, and Ser-205. These participate in hydrophobic, <scene name='Sandbox_34/Clik148ringstacking/2'>aromatic ring-stacking</scene>, and hydrogen bonding that effectively fill up the cleft between the two domains of papain.<ref> PMID:18598021 </ref>

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@@ Line 47: / Line 47: @@
 ==='''Cathepsin L'''===
-<scene name='Papain/Cathepsin_l/2'>Cathepsin L</scene>, another inhibitor of Papain, interacts with the <scene name='Papain/Cathepsin_l_interaction_w_pap/1'>residues</scene> Gln-19, Cys-25, Gly-66, Asp-158, and Trp-177 by hydrogen bonding them (Cathepsin L is illustrated in CPK coloring while the interacting sites of Papain are also shown in CPK). In addition to hydrogen bonding, hydrophobic interactions exist to exclude water, allowing the papain enzyme and Cathepsin L to associate even closer.  Finally, <scene name='Papain/Stacking_cathl/1'>Ring Stacking</scene> between Trp-177 and the Capthespin L molecule hold them tightly together.<ref>PMID:18598021</ref> Cathepsin L plays a role in many different diseases including malaria, leishmaniasis, Chagas' disease, African trypanosomiasis, toxoplasmosis, and amoebiasis. Some studies show that there is a relation between cathepsins and certain cancers, alzheimer's, and arthritis. <ref> PMID:20920298 </ref>
+<scene name='Papain/Cathepsin_l/2'>Cathepsin L</scene>, another inhibitor of Papain, is an endosomal cysteine protease that is believed to have both physiological and pathophysiological effects on the human body. It has been indicated not only in cancer, rhematoid  and osteo arthritis, and Alzheimer's, but its mechanism also appears similar to that of Ebola, SARS, Leishmania, malaria, Chagas' disease, African trypanosomiasis, toxoplasmosis, and amoebiasis.<ref> PMID:20920298 </ref>  Understanding the mechanism of inhibition through the use of papain is therefore crucial to developing treatments for such diseases.<ref> PMID:18499453 </ref> Cathepsin L interacts with the <scene name='Papain/Cathepsin_l_interaction_w_pap/1'>residues</scene> Gln-19, Cys-25, Gly-66, Asp-158, and Trp-177 by hydrogen bonding them (Cathepsin L is illustrated in CPK coloring while the interacting sites of Papain are also shown in CPK). In addition to hydrogen bonding, hydrophobic interactions exist to exclude water, allowing the papain enzyme and Cathepsin L to associate even closer.
+An interesting inhibitor for cathepsin L developed using papain as the model protease is that of <scene name='Sandbox_34/Clik148_inhibitor/2'>Clik-148</scene>.<ref> PMID:10600517 </ref> It forms a <scene name='Sandbox_34/Clik148_inhibit_cys25/1'>covalent ligand-bound cysteine protease complex</scene> with Cys-25. Five other residues are also involved in the bonding of Clik-148 to papain: Gln-19, Gly-66, Asp-158, Trp-177, and Ser-205. These participate in hydrophobic, <scene name='Sandbox_34/Clik148ringstacking/2'>aromatic ring-stacking</scene>, and hydrogen bonding that effectively fill up the cleft between the two domains of papain.<ref> PMID:18598021 </ref>
 ==='''Stefin B'''===