Design, Synthesis, Biological Activity, and Structural Analysis of Lactam‐Constrained PTPRJ Agonist Peptides
PTPRJ is a receptor‐like protein tyrosine phosphatase mainly known for its antiproliferative and tumor‐suppressive functions. PTPRJ dephosphorylates several growth factors and their receptors, negatively regulating cell proliferation and migration. We recently identified a disulfide‐bridged nonapept...
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| Veröffentlicht in: | ChemMedChem 2018-08, Vol.13 (16), p.1673-1680 |
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| creator | Sala, Marina Spensiero, Antonia Scala, Maria Carmina Pepe, Giacomo Bilotta, Anna Paduano, Francesco D'Agostino, Sabrina Lanzillotta, Delia Bertamino, Alessia Novellino, Ettore Trapasso, Francesco Gomez‐Monterrey, Isabel M. Campiglia, Pietro |
| description | PTPRJ is a receptor‐like protein tyrosine phosphatase mainly known for its antiproliferative and tumor‐suppressive functions. PTPRJ dephosphorylates several growth factors and their receptors, negatively regulating cell proliferation and migration. We recently identified a disulfide‐bridged nonapeptide, named PTPRJ‐19 (H‐[Cys‐His‐His‐Asn‐Leu‐Thr‐His‐Ala‐Cys]‐OH), which activates PTPRJ, thereby causing cell growth inhibition and apoptosis of both cancer and endothelial cells. With the aim of replacing the disulfide bridge by a chemically more stable moiety, we have synthesized and tested a series of lactam analogues of PTPRJ‐19. This replacement led to analogues with higher activity and greater stability than the parent peptide.
Disulfide vs. lactam: This work focused on the design and biological evaluation of PTPRJ agonist peptides. Derivatives of PTPRJ‐19 were generated by replacing the disulfide bridge chain with a lactam bridge. Our study provided a new derivative, peptide 7, with better anticancer cell growth activity and improved stability under various conditions. |
| doi_str_mv | 10.1002/cmdc.201800147 |
| format | Article |
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Disulfide vs. lactam: This work focused on the design and biological evaluation of PTPRJ agonist peptides. Derivatives of PTPRJ‐19 were generated by replacing the disulfide bridge chain with a lactam bridge. Our study provided a new derivative, peptide 7, with better anticancer cell growth activity and improved stability under various conditions.</description><identifier>ISSN: 1860-7179</identifier><identifier>EISSN: 1860-7187</identifier><identifier>DOI: 10.1002/cmdc.201800147</identifier><identifier>PMID: 29888867</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Amides ; Amino Acid Sequence ; Antineoplastic Agents - chemical synthesis ; Antineoplastic Agents - chemistry ; Antineoplastic Agents - pharmacology ; Apoptosis ; Biological activity ; Cancer ; Cell growth ; Cell proliferation ; Cell Proliferation - drug effects ; Chymotrypsin - chemistry ; Disulfide bonds ; Drug Design ; Drug Stability ; Endothelial cells ; Enzyme Activators - chemical synthesis ; Enzyme Activators - chemistry ; Enzyme Activators - pharmacology ; Growth factors ; HeLa Cells ; Humans ; lactam bridge ; Lactams - chemical synthesis ; Lactams - chemistry ; Lactams - pharmacology ; Molecular Structure ; Organic chemistry ; Peptides ; Peptides, Cyclic - chemical synthesis ; Peptides, Cyclic - chemistry ; Peptides, Cyclic - pharmacology ; phosphatases ; Protein-tyrosine-phosphatase ; Proteins ; Proteolysis ; Receptor-Like Protein Tyrosine Phosphatases, Class 3 - metabolism ; Receptors ; Structural analysis ; Trypsin - chemistry ; Tyrosine</subject><ispartof>ChemMedChem, 2018-08, Vol.13 (16), p.1673-1680</ispartof><rights>2018 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3737-944fc3ad732e02b544294fd025854ef76fbf67a9251e420aeba68038a3cb49b13</citedby><cites>FETCH-LOGICAL-c3737-944fc3ad732e02b544294fd025854ef76fbf67a9251e420aeba68038a3cb49b13</cites><orcidid>0000-0001-6521-7372 ; 0000-0001-9098-3191 ; 0000-0002-5482-6276 ; 0000-0002-7561-2023 ; 0000-0002-2877-0563 ; 0000-0003-0001-8748 ; 0000-0001-5848-873X ; 0000-0002-2181-2142 ; 0000-0003-0916-8101 ; 0000-0003-2739-7215 ; 0000-0002-1069-2181</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fcmdc.201800147$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fcmdc.201800147$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29888867$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sala, Marina</creatorcontrib><creatorcontrib>Spensiero, Antonia</creatorcontrib><creatorcontrib>Scala, Maria Carmina</creatorcontrib><creatorcontrib>Pepe, Giacomo</creatorcontrib><creatorcontrib>Bilotta, Anna</creatorcontrib><creatorcontrib>Paduano, Francesco</creatorcontrib><creatorcontrib>D'Agostino, Sabrina</creatorcontrib><creatorcontrib>Lanzillotta, Delia</creatorcontrib><creatorcontrib>Bertamino, Alessia</creatorcontrib><creatorcontrib>Novellino, Ettore</creatorcontrib><creatorcontrib>Trapasso, Francesco</creatorcontrib><creatorcontrib>Gomez‐Monterrey, Isabel M.</creatorcontrib><creatorcontrib>Campiglia, Pietro</creatorcontrib><title>Design, Synthesis, Biological Activity, and Structural Analysis of Lactam‐Constrained PTPRJ Agonist Peptides</title><title>ChemMedChem</title><addtitle>ChemMedChem</addtitle><description>PTPRJ is a receptor‐like protein tyrosine phosphatase mainly known for its antiproliferative and tumor‐suppressive functions. PTPRJ dephosphorylates several growth factors and their receptors, negatively regulating cell proliferation and migration. We recently identified a disulfide‐bridged nonapeptide, named PTPRJ‐19 (H‐[Cys‐His‐His‐Asn‐Leu‐Thr‐His‐Ala‐Cys]‐OH), which activates PTPRJ, thereby causing cell growth inhibition and apoptosis of both cancer and endothelial cells. With the aim of replacing the disulfide bridge by a chemically more stable moiety, we have synthesized and tested a series of lactam analogues of PTPRJ‐19. This replacement led to analogues with higher activity and greater stability than the parent peptide.
Disulfide vs. lactam: This work focused on the design and biological evaluation of PTPRJ agonist peptides. Derivatives of PTPRJ‐19 were generated by replacing the disulfide bridge chain with a lactam bridge. Our study provided a new derivative, peptide 7, with better anticancer cell growth activity and improved stability under various conditions.</description><subject>Amides</subject><subject>Amino Acid Sequence</subject><subject>Antineoplastic Agents - chemical synthesis</subject><subject>Antineoplastic Agents - chemistry</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Apoptosis</subject><subject>Biological activity</subject><subject>Cancer</subject><subject>Cell growth</subject><subject>Cell proliferation</subject><subject>Cell Proliferation - drug effects</subject><subject>Chymotrypsin - chemistry</subject><subject>Disulfide bonds</subject><subject>Drug Design</subject><subject>Drug Stability</subject><subject>Endothelial cells</subject><subject>Enzyme Activators - chemical synthesis</subject><subject>Enzyme Activators - chemistry</subject><subject>Enzyme Activators - pharmacology</subject><subject>Growth factors</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>lactam bridge</subject><subject>Lactams - chemical synthesis</subject><subject>Lactams - chemistry</subject><subject>Lactams - pharmacology</subject><subject>Molecular Structure</subject><subject>Organic chemistry</subject><subject>Peptides</subject><subject>Peptides, Cyclic - chemical synthesis</subject><subject>Peptides, Cyclic - chemistry</subject><subject>Peptides, Cyclic - pharmacology</subject><subject>phosphatases</subject><subject>Protein-tyrosine-phosphatase</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Receptor-Like Protein Tyrosine Phosphatases, Class 3 - metabolism</subject><subject>Receptors</subject><subject>Structural analysis</subject><subject>Trypsin - chemistry</subject><subject>Tyrosine</subject><issn>1860-7179</issn><issn>1860-7187</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0cuO0zAUBmALgZhhYMsSWWLDoi3Hl8T2smS4qoiKGdaR4zjFo8Tu2A4oOx6BZ-RJSNWhSGzwxkfy51-yf4SeElgRAPrSDK1ZUSASgHBxD50TWcJSECnun2ahztCjlG4AOJdEPkRnVMl5leIc-Uub3M4v8NXk89d5Tgv8yoU-7JzRPV6b7L65PC2w9i2-ynE0eYyHA6_7adY4dHijTdbDrx8_q-BTjtp52-Lt9fbzB7zeBe9Sxlu7z6616TF60Ok-2Sd3-wX68ub1dfVuufn09n213iwNE0wsFeedYboVjFqgTcE5VbxrgRay4LYTZdd0pdCKFsRyCto2upTApGam4aoh7AK9OObuY7gdbcr14JKxfa-9DWOqKRSMCipAzPT5P_QmjHF-3kEpUCUXjM1qdVQmhpSi7ep9dIOOU02gPjRRH5qoT03MF57dxY7NYNsT__P1M1BH8N31dvpPXF19vKz-hv8Gu1KVTQ</recordid><startdate>20180820</startdate><enddate>20180820</enddate><creator>Sala, Marina</creator><creator>Spensiero, Antonia</creator><creator>Scala, Maria Carmina</creator><creator>Pepe, Giacomo</creator><creator>Bilotta, Anna</creator><creator>Paduano, Francesco</creator><creator>D'Agostino, Sabrina</creator><creator>Lanzillotta, Delia</creator><creator>Bertamino, Alessia</creator><creator>Novellino, Ettore</creator><creator>Trapasso, Francesco</creator><creator>Gomez‐Monterrey, Isabel M.</creator><creator>Campiglia, Pietro</creator><general>Wiley Subscription Services, Inc</general><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>7TK</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-6521-7372</orcidid><orcidid>https://orcid.org/0000-0001-9098-3191</orcidid><orcidid>https://orcid.org/0000-0002-5482-6276</orcidid><orcidid>https://orcid.org/0000-0002-7561-2023</orcidid><orcidid>https://orcid.org/0000-0002-2877-0563</orcidid><orcidid>https://orcid.org/0000-0003-0001-8748</orcidid><orcidid>https://orcid.org/0000-0001-5848-873X</orcidid><orcidid>https://orcid.org/0000-0002-2181-2142</orcidid><orcidid>https://orcid.org/0000-0003-0916-8101</orcidid><orcidid>https://orcid.org/0000-0003-2739-7215</orcidid><orcidid>https://orcid.org/0000-0002-1069-2181</orcidid></search><sort><creationdate>20180820</creationdate><title>Design, Synthesis, Biological Activity, and Structural Analysis of Lactam‐Constrained PTPRJ Agonist Peptides</title><author>Sala, Marina ; Spensiero, Antonia ; Scala, Maria Carmina ; Pepe, Giacomo ; Bilotta, Anna ; Paduano, Francesco ; D'Agostino, Sabrina ; Lanzillotta, Delia ; Bertamino, Alessia ; Novellino, Ettore ; Trapasso, Francesco ; Gomez‐Monterrey, Isabel M. ; Campiglia, Pietro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3737-944fc3ad732e02b544294fd025854ef76fbf67a9251e420aeba68038a3cb49b13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Amides</topic><topic>Amino Acid Sequence</topic><topic>Antineoplastic Agents - chemical synthesis</topic><topic>Antineoplastic Agents - chemistry</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Apoptosis</topic><topic>Biological activity</topic><topic>Cancer</topic><topic>Cell growth</topic><topic>Cell proliferation</topic><topic>Cell Proliferation - drug effects</topic><topic>Chymotrypsin - chemistry</topic><topic>Disulfide bonds</topic><topic>Drug Design</topic><topic>Drug Stability</topic><topic>Endothelial cells</topic><topic>Enzyme Activators - chemical synthesis</topic><topic>Enzyme Activators - chemistry</topic><topic>Enzyme Activators - pharmacology</topic><topic>Growth factors</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>lactam bridge</topic><topic>Lactams - chemical synthesis</topic><topic>Lactams - chemistry</topic><topic>Lactams - pharmacology</topic><topic>Molecular Structure</topic><topic>Organic chemistry</topic><topic>Peptides</topic><topic>Peptides, Cyclic - chemical synthesis</topic><topic>Peptides, Cyclic - chemistry</topic><topic>Peptides, Cyclic - pharmacology</topic><topic>phosphatases</topic><topic>Protein-tyrosine-phosphatase</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Receptor-Like Protein Tyrosine Phosphatases, Class 3 - metabolism</topic><topic>Receptors</topic><topic>Structural analysis</topic><topic>Trypsin - chemistry</topic><topic>Tyrosine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sala, Marina</creatorcontrib><creatorcontrib>Spensiero, Antonia</creatorcontrib><creatorcontrib>Scala, Maria Carmina</creatorcontrib><creatorcontrib>Pepe, Giacomo</creatorcontrib><creatorcontrib>Bilotta, Anna</creatorcontrib><creatorcontrib>Paduano, Francesco</creatorcontrib><creatorcontrib>D'Agostino, Sabrina</creatorcontrib><creatorcontrib>Lanzillotta, Delia</creatorcontrib><creatorcontrib>Bertamino, Alessia</creatorcontrib><creatorcontrib>Novellino, Ettore</creatorcontrib><creatorcontrib>Trapasso, Francesco</creatorcontrib><creatorcontrib>Gomez‐Monterrey, Isabel M.</creatorcontrib><creatorcontrib>Campiglia, Pietro</creatorcontrib><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>Neurosciences Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>ChemMedChem</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sala, Marina</au><au>Spensiero, Antonia</au><au>Scala, Maria Carmina</au><au>Pepe, Giacomo</au><au>Bilotta, Anna</au><au>Paduano, Francesco</au><au>D'Agostino, Sabrina</au><au>Lanzillotta, Delia</au><au>Bertamino, Alessia</au><au>Novellino, Ettore</au><au>Trapasso, Francesco</au><au>Gomez‐Monterrey, Isabel M.</au><au>Campiglia, Pietro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Design, Synthesis, Biological Activity, and Structural Analysis of Lactam‐Constrained PTPRJ Agonist Peptides</atitle><jtitle>ChemMedChem</jtitle><addtitle>ChemMedChem</addtitle><date>2018-08-20</date><risdate>2018</risdate><volume>13</volume><issue>16</issue><spage>1673</spage><epage>1680</epage><pages>1673-1680</pages><issn>1860-7179</issn><eissn>1860-7187</eissn><abstract>PTPRJ is a receptor‐like protein tyrosine phosphatase mainly known for its antiproliferative and tumor‐suppressive functions. PTPRJ dephosphorylates several growth factors and their receptors, negatively regulating cell proliferation and migration. We recently identified a disulfide‐bridged nonapeptide, named PTPRJ‐19 (H‐[Cys‐His‐His‐Asn‐Leu‐Thr‐His‐Ala‐Cys]‐OH), which activates PTPRJ, thereby causing cell growth inhibition and apoptosis of both cancer and endothelial cells. With the aim of replacing the disulfide bridge by a chemically more stable moiety, we have synthesized and tested a series of lactam analogues of PTPRJ‐19. This replacement led to analogues with higher activity and greater stability than the parent peptide.
Disulfide vs. lactam: This work focused on the design and biological evaluation of PTPRJ agonist peptides. Derivatives of PTPRJ‐19 were generated by replacing the disulfide bridge chain with a lactam bridge. Our study provided a new derivative, peptide 7, with better anticancer cell growth activity and improved stability under various conditions.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>29888867</pmid><doi>10.1002/cmdc.201800147</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0001-6521-7372</orcidid><orcidid>https://orcid.org/0000-0001-9098-3191</orcidid><orcidid>https://orcid.org/0000-0002-5482-6276</orcidid><orcidid>https://orcid.org/0000-0002-7561-2023</orcidid><orcidid>https://orcid.org/0000-0002-2877-0563</orcidid><orcidid>https://orcid.org/0000-0003-0001-8748</orcidid><orcidid>https://orcid.org/0000-0001-5848-873X</orcidid><orcidid>https://orcid.org/0000-0002-2181-2142</orcidid><orcidid>https://orcid.org/0000-0003-0916-8101</orcidid><orcidid>https://orcid.org/0000-0003-2739-7215</orcidid><orcidid>https://orcid.org/0000-0002-1069-2181</orcidid></addata></record> |
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| subjects | Amides Amino Acid Sequence Antineoplastic Agents - chemical synthesis Antineoplastic Agents - chemistry Antineoplastic Agents - pharmacology Apoptosis Biological activity Cancer Cell growth Cell proliferation Cell Proliferation - drug effects Chymotrypsin - chemistry Disulfide bonds Drug Design Drug Stability Endothelial cells Enzyme Activators - chemical synthesis Enzyme Activators - chemistry Enzyme Activators - pharmacology Growth factors HeLa Cells Humans lactam bridge Lactams - chemical synthesis Lactams - chemistry Lactams - pharmacology Molecular Structure Organic chemistry Peptides Peptides, Cyclic - chemical synthesis Peptides, Cyclic - chemistry Peptides, Cyclic - pharmacology phosphatases Protein-tyrosine-phosphatase Proteins Proteolysis Receptor-Like Protein Tyrosine Phosphatases, Class 3 - metabolism Receptors Structural analysis Trypsin - chemistry Tyrosine |
| title | Design, Synthesis, Biological Activity, and Structural Analysis of Lactam‐Constrained PTPRJ Agonist Peptides |
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