Loading…
P3 and P4 position analysis of vinyl ester pseudopeptide proteasome inhibitors
Here following is the report on the use of small, focused libraries to study P3 and P4 positions of vinyl ester pseudopeptides, selective inhibitors for trypsin-like activity of the 20S proteasome. Two small libraries of tripeptidic-based vinyl ester derivative proteasome inhibitors were synthesized...
Saved in:
| Published in: | Bioorganic & medicinal chemistry letters 2006-06, Vol.16 (12), p.3125-3130 |
|---|---|
| Main Authors: | , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c415t-8979c1b4f7145a2db01eab842401973579ed7b291bf6a313e9599c7c9fc06be13 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c415t-8979c1b4f7145a2db01eab842401973579ed7b291bf6a313e9599c7c9fc06be13 |
| container_end_page | 3130 |
| container_issue | 12 |
| container_start_page | 3125 |
| container_title | Bioorganic & medicinal chemistry letters |
| container_volume | 16 |
| creator | Marastoni, Mauro Baldisserotto, Anna Trapella, Claudio Gavioli, Riccardo Tomatis, Roberto |
| description | Here following is the report on the use of small, focused libraries to study P3 and P4 positions of vinyl ester pseudopeptides, selective inhibitors for trypsin-like activity of the 20S proteasome.
Two small libraries of tripeptidic-based vinyl ester derivative proteasome inhibitors were synthesized and tested, starting with the Hmb-Val-Gln-Leu-VE prototype. The P3 and P4 positions were investigated with a complete set of amino acid residues, some of which showed remarkable selective inhibition of the trypsin-like (β2) subunit. In both positions, aromatic and hydrophobic residues were preferred. |
| doi_str_mv | 10.1016/j.bmcl.2006.03.070 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67936554</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0960894X06003696</els_id><sourcerecordid>67936554</sourcerecordid><originalsourceid>FETCH-LOGICAL-c415t-8979c1b4f7145a2db01eab842401973579ed7b291bf6a313e9599c7c9fc06be13</originalsourceid><addsrcrecordid>eNqFkEtr3DAUhUVpaaZJ_0AXRZt2N-6V9bKgmxLSB4QmixSyE5J8TTXYlit5AvPvq2EGsmtXlwvfORw-Qt4xaBgw9WnX-CmMTQugGuANaHhBNkwoseUC5EuyAaNg2xnxeEHelLIDYAKEeE0umFLAueg25Oc9p27u6b2gSypxjWmuvxsPJRaaBvoU58NIsayY6VJw36cFlzX2SJecVnQlTUjj_Dv6uKZcrsirwY0F357vJfn19ebh-vv29u7bj-svt9sgmFzrJm0C82LQTEjX9h4YOt-JVgAzmkttsNe-NcwPynHG0Uhjgg5mCKA8Mn5JPp5664o_-zrPTrEEHEc3Y9oXq7ThSkrxX5BppjqjjmB7AkNOpWQc7JLj5PLBMrBH3XZnj7rtUbcFbqvuGnp_bt_7CfvnyNlvBT6cAVeCG4fs5hDLM6e17DqpKvf5xGGV9hQx2xIizgH7mDGstk_xXzv-AlPJnYU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17168964</pqid></control><display><type>article</type><title>P3 and P4 position analysis of vinyl ester pseudopeptide proteasome inhibitors</title><source>ScienceDirect Freedom Collection</source><creator>Marastoni, Mauro ; Baldisserotto, Anna ; Trapella, Claudio ; Gavioli, Riccardo ; Tomatis, Roberto</creator><creatorcontrib>Marastoni, Mauro ; Baldisserotto, Anna ; Trapella, Claudio ; Gavioli, Riccardo ; Tomatis, Roberto</creatorcontrib><description>Here following is the report on the use of small, focused libraries to study P3 and P4 positions of vinyl ester pseudopeptides, selective inhibitors for trypsin-like activity of the 20S proteasome.
Two small libraries of tripeptidic-based vinyl ester derivative proteasome inhibitors were synthesized and tested, starting with the Hmb-Val-Gln-Leu-VE prototype. The P3 and P4 positions were investigated with a complete set of amino acid residues, some of which showed remarkable selective inhibition of the trypsin-like (β2) subunit. In both positions, aromatic and hydrophobic residues were preferred.</description><identifier>ISSN: 0960-894X</identifier><identifier>EISSN: 1464-3405</identifier><identifier>DOI: 10.1016/j.bmcl.2006.03.070</identifier><identifier>PMID: 16603348</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Biological and medical sciences ; Esters - chemistry ; Medical sciences ; Miscellaneous ; Peptides - chemical synthesis ; Peptides - chemistry ; Peptides - pharmacology ; Pharmacology. Drug treatments ; Proteasome Endopeptidase Complex - metabolism ; Proteasome Inhibitors ; Small libraries ; Solid-phase synthesis ; Trypsin-like activity ; Vinyl Compounds - chemistry</subject><ispartof>Bioorganic & medicinal chemistry letters, 2006-06, Vol.16 (12), p.3125-3130</ispartof><rights>2006 Elsevier Ltd</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-8979c1b4f7145a2db01eab842401973579ed7b291bf6a313e9599c7c9fc06be13</citedby><cites>FETCH-LOGICAL-c415t-8979c1b4f7145a2db01eab842401973579ed7b291bf6a313e9599c7c9fc06be13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17758856$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16603348$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Marastoni, Mauro</creatorcontrib><creatorcontrib>Baldisserotto, Anna</creatorcontrib><creatorcontrib>Trapella, Claudio</creatorcontrib><creatorcontrib>Gavioli, Riccardo</creatorcontrib><creatorcontrib>Tomatis, Roberto</creatorcontrib><title>P3 and P4 position analysis of vinyl ester pseudopeptide proteasome inhibitors</title><title>Bioorganic & medicinal chemistry letters</title><addtitle>Bioorg Med Chem Lett</addtitle><description>Here following is the report on the use of small, focused libraries to study P3 and P4 positions of vinyl ester pseudopeptides, selective inhibitors for trypsin-like activity of the 20S proteasome.
Two small libraries of tripeptidic-based vinyl ester derivative proteasome inhibitors were synthesized and tested, starting with the Hmb-Val-Gln-Leu-VE prototype. The P3 and P4 positions were investigated with a complete set of amino acid residues, some of which showed remarkable selective inhibition of the trypsin-like (β2) subunit. In both positions, aromatic and hydrophobic residues were preferred.</description><subject>Amino Acid Sequence</subject><subject>Biological and medical sciences</subject><subject>Esters - chemistry</subject><subject>Medical sciences</subject><subject>Miscellaneous</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Peptides - pharmacology</subject><subject>Pharmacology. Drug treatments</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>Proteasome Inhibitors</subject><subject>Small libraries</subject><subject>Solid-phase synthesis</subject><subject>Trypsin-like activity</subject><subject>Vinyl Compounds - chemistry</subject><issn>0960-894X</issn><issn>1464-3405</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNqFkEtr3DAUhUVpaaZJ_0AXRZt2N-6V9bKgmxLSB4QmixSyE5J8TTXYlit5AvPvq2EGsmtXlwvfORw-Qt4xaBgw9WnX-CmMTQugGuANaHhBNkwoseUC5EuyAaNg2xnxeEHelLIDYAKEeE0umFLAueg25Oc9p27u6b2gSypxjWmuvxsPJRaaBvoU58NIsayY6VJw36cFlzX2SJecVnQlTUjj_Dv6uKZcrsirwY0F357vJfn19ebh-vv29u7bj-svt9sgmFzrJm0C82LQTEjX9h4YOt-JVgAzmkttsNe-NcwPynHG0Uhjgg5mCKA8Mn5JPp5664o_-zrPTrEEHEc3Y9oXq7ThSkrxX5BppjqjjmB7AkNOpWQc7JLj5PLBMrBH3XZnj7rtUbcFbqvuGnp_bt_7CfvnyNlvBT6cAVeCG4fs5hDLM6e17DqpKvf5xGGV9hQx2xIizgH7mDGstk_xXzv-AlPJnYU</recordid><startdate>20060615</startdate><enddate>20060615</enddate><creator>Marastoni, Mauro</creator><creator>Baldisserotto, Anna</creator><creator>Trapella, Claudio</creator><creator>Gavioli, Riccardo</creator><creator>Tomatis, Roberto</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20060615</creationdate><title>P3 and P4 position analysis of vinyl ester pseudopeptide proteasome inhibitors</title><author>Marastoni, Mauro ; Baldisserotto, Anna ; Trapella, Claudio ; Gavioli, Riccardo ; Tomatis, Roberto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-8979c1b4f7145a2db01eab842401973579ed7b291bf6a313e9599c7c9fc06be13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Biological and medical sciences</topic><topic>Esters - chemistry</topic><topic>Medical sciences</topic><topic>Miscellaneous</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Peptides - pharmacology</topic><topic>Pharmacology. Drug treatments</topic><topic>Proteasome Endopeptidase Complex - metabolism</topic><topic>Proteasome Inhibitors</topic><topic>Small libraries</topic><topic>Solid-phase synthesis</topic><topic>Trypsin-like activity</topic><topic>Vinyl Compounds - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marastoni, Mauro</creatorcontrib><creatorcontrib>Baldisserotto, Anna</creatorcontrib><creatorcontrib>Trapella, Claudio</creatorcontrib><creatorcontrib>Gavioli, Riccardo</creatorcontrib><creatorcontrib>Tomatis, Roberto</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Marastoni, Mauro</au><au>Baldisserotto, Anna</au><au>Trapella, Claudio</au><au>Gavioli, Riccardo</au><au>Tomatis, Roberto</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>P3 and P4 position analysis of vinyl ester pseudopeptide proteasome inhibitors</atitle><jtitle>Bioorganic & medicinal chemistry letters</jtitle><addtitle>Bioorg Med Chem Lett</addtitle><date>2006-06-15</date><risdate>2006</risdate><volume>16</volume><issue>12</issue><spage>3125</spage><epage>3130</epage><pages>3125-3130</pages><issn>0960-894X</issn><eissn>1464-3405</eissn><abstract>Here following is the report on the use of small, focused libraries to study P3 and P4 positions of vinyl ester pseudopeptides, selective inhibitors for trypsin-like activity of the 20S proteasome.
Two small libraries of tripeptidic-based vinyl ester derivative proteasome inhibitors were synthesized and tested, starting with the Hmb-Val-Gln-Leu-VE prototype. The P3 and P4 positions were investigated with a complete set of amino acid residues, some of which showed remarkable selective inhibition of the trypsin-like (β2) subunit. In both positions, aromatic and hydrophobic residues were preferred.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>16603348</pmid><doi>10.1016/j.bmcl.2006.03.070</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0960-894X |
| ispartof | Bioorganic & medicinal chemistry letters, 2006-06, Vol.16 (12), p.3125-3130 |
| issn | 0960-894X 1464-3405 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_67936554 |
| source | ScienceDirect Freedom Collection |
| subjects | Amino Acid Sequence Biological and medical sciences Esters - chemistry Medical sciences Miscellaneous Peptides - chemical synthesis Peptides - chemistry Peptides - pharmacology Pharmacology. Drug treatments Proteasome Endopeptidase Complex - metabolism Proteasome Inhibitors Small libraries Solid-phase synthesis Trypsin-like activity Vinyl Compounds - chemistry |
| title | P3 and P4 position analysis of vinyl ester pseudopeptide proteasome inhibitors |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T05%3A32%3A37IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=P3%20and%20P4%20position%20analysis%20of%20vinyl%20ester%20pseudopeptide%20proteasome%20inhibitors&rft.jtitle=Bioorganic%20&%20medicinal%20chemistry%20letters&rft.au=Marastoni,%20Mauro&rft.date=2006-06-15&rft.volume=16&rft.issue=12&rft.spage=3125&rft.epage=3130&rft.pages=3125-3130&rft.issn=0960-894X&rft.eissn=1464-3405&rft_id=info:doi/10.1016/j.bmcl.2006.03.070&rft_dat=%3Cproquest_cross%3E67936554%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c415t-8979c1b4f7145a2db01eab842401973579ed7b291bf6a313e9599c7c9fc06be13%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=17168964&rft_id=info:pmid/16603348&rfr_iscdi=true |