Discovery and structure–activity relationships of small molecules that block the human immunoglobulin G–human neonatal Fc receptor (hIgG–hFcRn) protein–protein interaction
The neonatal Fc receptor, FcRn, prolongs the half-life of IgG in the serum and represents a potential therapeutic target for the treatment of autoimmune disease. Small molecules that block the protein–protein interactions of human IgG–human FcRn may lower pathogenic autoantibodies and provide effect...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry letters 2013-03, Vol.23 (5), p.1253-1256 |
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| container_end_page | 1256 |
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| container_title | Bioorganic & medicinal chemistry letters |
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| creator | Wang, Zhaolin Fraley, Cara Mezo, Adam R. |
| description | The neonatal Fc receptor, FcRn, prolongs the half-life of IgG in the serum and represents a potential therapeutic target for the treatment of autoimmune disease. Small molecules that block the protein–protein interactions of human IgG–human FcRn may lower pathogenic autoantibodies and provide effective treatment. A novel class of quinoxalines has been discovered as antagonists of the IgG:FcRn protein–protein interaction through optimization of a hit derived from a virtual ligand-based screen. |
| doi_str_mv | 10.1016/j.bmcl.2013.01.014 |
| format | Article |
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Small molecules that block the protein–protein interactions of human IgG–human FcRn may lower pathogenic autoantibodies and provide effective treatment. A novel class of quinoxalines has been discovered as antagonists of the IgG:FcRn protein–protein interaction through optimization of a hit derived from a virtual ligand-based screen.</description><identifier>ISSN: 0960-894X</identifier><identifier>EISSN: 1464-3405</identifier><identifier>DOI: 10.1016/j.bmcl.2013.01.014</identifier><identifier>PMID: 23375228</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>antagonists ; autoantibodies ; blood serum ; Drug Evaluation, Preclinical ; FcRn ; half life ; Histocompatibility Antigens Class I - immunology ; Histocompatibility Antigens Class I - metabolism ; Humans ; immunoglobulin G ; Immunoglobulin G - immunology ; Immunoglobulin G - metabolism ; Inhibitor ; Ligands ; Neonatal Fc receptor ; Protein Interaction Domains and Motifs - drug effects ; Protein–protein interactions ; quinoxalines ; Quinoxalines - pharmacology ; Receptors, Fc - antagonists & inhibitors ; Receptors, Fc - immunology ; Receptors, Fc - metabolism ; Small molecule ; Structure-Activity Relationship ; structure-activity relationships</subject><ispartof>Bioorganic & medicinal chemistry letters, 2013-03, Vol.23 (5), p.1253-1256</ispartof><rights>2013 Elsevier Ltd</rights><rights>Copyright © 2013 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c380t-e8aee12c5619fc580bd55f52219cad7f98bf444cb794e135165076773d5b5da3</citedby><cites>FETCH-LOGICAL-c380t-e8aee12c5619fc580bd55f52219cad7f98bf444cb794e135165076773d5b5da3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0960894X1300036X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23375228$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Zhaolin</creatorcontrib><creatorcontrib>Fraley, Cara</creatorcontrib><creatorcontrib>Mezo, Adam R.</creatorcontrib><title>Discovery and structure–activity relationships of small molecules that block the human immunoglobulin G–human neonatal Fc receptor (hIgG–hFcRn) protein–protein interaction</title><title>Bioorganic & medicinal chemistry letters</title><addtitle>Bioorg Med Chem Lett</addtitle><description>The neonatal Fc receptor, FcRn, prolongs the half-life of IgG in the serum and represents a potential therapeutic target for the treatment of autoimmune disease. Small molecules that block the protein–protein interactions of human IgG–human FcRn may lower pathogenic autoantibodies and provide effective treatment. A novel class of quinoxalines has been discovered as antagonists of the IgG:FcRn protein–protein interaction through optimization of a hit derived from a virtual ligand-based screen.</description><subject>antagonists</subject><subject>autoantibodies</subject><subject>blood serum</subject><subject>Drug Evaluation, Preclinical</subject><subject>FcRn</subject><subject>half life</subject><subject>Histocompatibility Antigens Class I - immunology</subject><subject>Histocompatibility Antigens Class I - metabolism</subject><subject>Humans</subject><subject>immunoglobulin G</subject><subject>Immunoglobulin G - immunology</subject><subject>Immunoglobulin G - metabolism</subject><subject>Inhibitor</subject><subject>Ligands</subject><subject>Neonatal Fc receptor</subject><subject>Protein Interaction Domains and Motifs - drug effects</subject><subject>Protein–protein interactions</subject><subject>quinoxalines</subject><subject>Quinoxalines - pharmacology</subject><subject>Receptors, Fc - antagonists & inhibitors</subject><subject>Receptors, Fc - immunology</subject><subject>Receptors, Fc - metabolism</subject><subject>Small molecule</subject><subject>Structure-Activity Relationship</subject><subject>structure-activity relationships</subject><issn>0960-894X</issn><issn>1464-3405</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc-KFDEQxoMo7uzqC3jQHHcPPSadpP-AF1mddWFB0BW8hXS6eiZjOplN0gNz8x18FN_IJzHtjB6FghSVX31U1YfQC0qWlNDq9XbZjdouS0LZktAc_BFaUF7xgnEiHqMFaStSNC3_eobOY9ySTBDOn6KzkrFalGWzQD_fmaj9HsIBK9fjmMKk0xTg1_cfSiezN-mAA1iVjHdxY3YR-wHHUVmLR29BTxYiThuVcGe9_pZTwJtpVA6bcZycX1vfTdY4fJMVjx8OvFNJWbzSWVrDLvmALze36z_ISn9yV3gXfALjcuGUYeMShHkk756hJ4OyEZ6f3gt0v3p_f_2huPt4c3v99q7QrCGpgEYB0FKLiraDFg3peiGGvDZtterroW26gXOuu7rlQJmglSB1VdesF53oFbtAl0fZPMLDBDHJMd8KrFV5gylKWjYNIw2reEbLI6qDjzHAIHfBjCocJCVy9kpu5eyVnL2ShOaYm16e9KduhP5fy19zMvDqCAzKS7UOJsovn7OCyEYyWrU0E2-OBOQz7A0EGbUBp6E3-bJJ9t78b4LfALe3Kw</recordid><startdate>20130301</startdate><enddate>20130301</enddate><creator>Wang, Zhaolin</creator><creator>Fraley, Cara</creator><creator>Mezo, Adam R.</creator><general>Elsevier Ltd</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20130301</creationdate><title>Discovery and structure–activity relationships of small molecules that block the human immunoglobulin G–human neonatal Fc receptor (hIgG–hFcRn) protein–protein interaction</title><author>Wang, Zhaolin ; Fraley, Cara ; Mezo, Adam R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c380t-e8aee12c5619fc580bd55f52219cad7f98bf444cb794e135165076773d5b5da3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>antagonists</topic><topic>autoantibodies</topic><topic>blood serum</topic><topic>Drug Evaluation, Preclinical</topic><topic>FcRn</topic><topic>half life</topic><topic>Histocompatibility Antigens Class I - immunology</topic><topic>Histocompatibility Antigens Class I - metabolism</topic><topic>Humans</topic><topic>immunoglobulin G</topic><topic>Immunoglobulin G - immunology</topic><topic>Immunoglobulin G - metabolism</topic><topic>Inhibitor</topic><topic>Ligands</topic><topic>Neonatal Fc receptor</topic><topic>Protein Interaction Domains and Motifs - drug effects</topic><topic>Protein–protein interactions</topic><topic>quinoxalines</topic><topic>Quinoxalines - pharmacology</topic><topic>Receptors, Fc - antagonists & inhibitors</topic><topic>Receptors, Fc - immunology</topic><topic>Receptors, Fc - metabolism</topic><topic>Small molecule</topic><topic>Structure-Activity Relationship</topic><topic>structure-activity relationships</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Zhaolin</creatorcontrib><creatorcontrib>Fraley, Cara</creatorcontrib><creatorcontrib>Mezo, Adam R.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Zhaolin</au><au>Fraley, Cara</au><au>Mezo, Adam R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Discovery and structure–activity relationships of small molecules that block the human immunoglobulin G–human neonatal Fc receptor (hIgG–hFcRn) protein–protein interaction</atitle><jtitle>Bioorganic & medicinal chemistry letters</jtitle><addtitle>Bioorg Med Chem Lett</addtitle><date>2013-03-01</date><risdate>2013</risdate><volume>23</volume><issue>5</issue><spage>1253</spage><epage>1256</epage><pages>1253-1256</pages><issn>0960-894X</issn><eissn>1464-3405</eissn><abstract>The neonatal Fc receptor, FcRn, prolongs the half-life of IgG in the serum and represents a potential therapeutic target for the treatment of autoimmune disease. Small molecules that block the protein–protein interactions of human IgG–human FcRn may lower pathogenic autoantibodies and provide effective treatment. A novel class of quinoxalines has been discovered as antagonists of the IgG:FcRn protein–protein interaction through optimization of a hit derived from a virtual ligand-based screen.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>23375228</pmid><doi>10.1016/j.bmcl.2013.01.014</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0960-894X |
| ispartof | Bioorganic & medicinal chemistry letters, 2013-03, Vol.23 (5), p.1253-1256 |
| issn | 0960-894X 1464-3405 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | antagonists autoantibodies blood serum Drug Evaluation, Preclinical FcRn half life Histocompatibility Antigens Class I - immunology Histocompatibility Antigens Class I - metabolism Humans immunoglobulin G Immunoglobulin G - immunology Immunoglobulin G - metabolism Inhibitor Ligands Neonatal Fc receptor Protein Interaction Domains and Motifs - drug effects Protein–protein interactions quinoxalines Quinoxalines - pharmacology Receptors, Fc - antagonists & inhibitors Receptors, Fc - immunology Receptors, Fc - metabolism Small molecule Structure-Activity Relationship structure-activity relationships |
| title | Discovery and structure–activity relationships of small molecules that block the human immunoglobulin G–human neonatal Fc receptor (hIgG–hFcRn) protein–protein interaction |
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