Discovery of Antitumor Active Peptides Derived from Peroxiredoxin 5
The peroxiredoxin 5 (PRDX5) is a member of peroxiredoxins with antitumor activity. However, as a recombinant protein, PRDX5 is restricted in clinic due to high cost and keeping high dose in medication. The alternative way is to explore the antitumor active fragments of PRDX5 for potential of peptide...
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| Veröffentlicht in: | ChemMedChem 2021-11, Vol.16 (22), p.3477-3483 |
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| creator | Liu, Juanjuan Zou, Sen Zhang, Yan Lin, Ru Duan, Yanbo He, Weiqing Yang, Zhaoyong |
| description | The peroxiredoxin 5 (PRDX5) is a member of peroxiredoxins with antitumor activity. However, as a recombinant protein, PRDX5 is restricted in clinic due to high cost and keeping high dose in medication. The alternative way is to explore the antitumor active fragments of PRDX5 for potential of peptide drugs. According to the sequence, crystal structure and enzyme function of PRDX5, seven peptides were designed and named as IMB‐P1∼7. The peptide IMB‐P1 (AFTPGCSKTHLPGFVEQAEAL) containing critical residue C47 exhibited antitumor activity similar to PRDX5 in vivo. Transcriptome analysis showed peptide IMB‐P1 could make influence on expression of multiple genes involved in tumorigenesis and deterioration. Besides, an important discovery is the down‐regulation of oxidation‐related genes. In CT26 cells, IMB‐P1 carried similar antitumor activity with increasing ROS level to intact PRDX5. The results demonstrated that peptide IMB‐P1 with easier synthesis from PRDX5 may serve as a promising antitumor candidate.
Fully functional fragment: Seven peptides were designed in accordance with the sequence, crystal structure, and enzyme function of PRDX5. The peptide IMB‐P1 (AFTPGCSKTHLPGFVEQAEAL) containing the critical residue C47 was found to retain similar antitumor activity as that of intact PRDX5 protein in vivo and in vitro. |
| doi_str_mv | 10.1002/cmdc.202100323 |
| format | Article |
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Fully functional fragment: Seven peptides were designed in accordance with the sequence, crystal structure, and enzyme function of PRDX5. The peptide IMB‐P1 (AFTPGCSKTHLPGFVEQAEAL) containing the critical residue C47 was found to retain similar antitumor activity as that of intact PRDX5 protein in vivo and in vitro.</description><identifier>ISSN: 1860-7179</identifier><identifier>EISSN: 1860-7187</identifier><identifier>DOI: 10.1002/cmdc.202100323</identifier><identifier>PMID: 34313010</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Amino Acid Sequence ; Anticancer properties ; Antineoplastic Agents - chemical synthesis ; Antineoplastic Agents - chemistry ; Antineoplastic Agents - pharmacology ; antioxidation ; Antitumor activity ; antitumor agents ; Cell Line, Tumor ; Cell Proliferation - drug effects ; Cell Survival - drug effects ; Crystal structure ; Drug Screening Assays, Antitumor ; Gene expression ; Gene regulation ; Genes ; Humans ; Oxidation ; Peptides ; Peptides - chemical synthesis ; Peptides - chemistry ; Peptides - pharmacology ; Peroxiredoxin ; peroxiredoxin-5 ; Peroxiredoxins - chemistry ; Protein Conformation ; Sequence Alignment ; Structure-function relationships ; transcriptome analysis ; Transcriptomes ; Tumorigenesis</subject><ispartof>ChemMedChem, 2021-11, Vol.16 (22), p.3477-3483</ispartof><rights>2021 Wiley‐VCH GmbH</rights><rights>2021 Wiley-VCH GmbH.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3733-9a84d481f162519e814d082594eb5b4973428663b1ad3e19ec9c3ce2eb65c3ff3</citedby><cites>FETCH-LOGICAL-c3733-9a84d481f162519e814d082594eb5b4973428663b1ad3e19ec9c3ce2eb65c3ff3</cites></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.202100323$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fcmdc.202100323$$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/34313010$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Juanjuan</creatorcontrib><creatorcontrib>Zou, Sen</creatorcontrib><creatorcontrib>Zhang, Yan</creatorcontrib><creatorcontrib>Lin, Ru</creatorcontrib><creatorcontrib>Duan, Yanbo</creatorcontrib><creatorcontrib>He, Weiqing</creatorcontrib><creatorcontrib>Yang, Zhaoyong</creatorcontrib><title>Discovery of Antitumor Active Peptides Derived from Peroxiredoxin 5</title><title>ChemMedChem</title><addtitle>ChemMedChem</addtitle><description>The peroxiredoxin 5 (PRDX5) is a member of peroxiredoxins with antitumor activity. However, as a recombinant protein, PRDX5 is restricted in clinic due to high cost and keeping high dose in medication. The alternative way is to explore the antitumor active fragments of PRDX5 for potential of peptide drugs. According to the sequence, crystal structure and enzyme function of PRDX5, seven peptides were designed and named as IMB‐P1∼7. The peptide IMB‐P1 (AFTPGCSKTHLPGFVEQAEAL) containing critical residue C47 exhibited antitumor activity similar to PRDX5 in vivo. Transcriptome analysis showed peptide IMB‐P1 could make influence on expression of multiple genes involved in tumorigenesis and deterioration. Besides, an important discovery is the down‐regulation of oxidation‐related genes. In CT26 cells, IMB‐P1 carried similar antitumor activity with increasing ROS level to intact PRDX5. The results demonstrated that peptide IMB‐P1 with easier synthesis from PRDX5 may serve as a promising antitumor candidate.
Fully functional fragment: Seven peptides were designed in accordance with the sequence, crystal structure, and enzyme function of PRDX5. The peptide IMB‐P1 (AFTPGCSKTHLPGFVEQAEAL) containing the critical residue C47 was found to retain similar antitumor activity as that of intact PRDX5 protein in vivo and in vitro.</description><subject>Amino Acid Sequence</subject><subject>Anticancer properties</subject><subject>Antineoplastic Agents - chemical synthesis</subject><subject>Antineoplastic Agents - chemistry</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>antioxidation</subject><subject>Antitumor activity</subject><subject>antitumor agents</subject><subject>Cell Line, Tumor</subject><subject>Cell Proliferation - drug effects</subject><subject>Cell Survival - drug effects</subject><subject>Crystal structure</subject><subject>Drug Screening Assays, Antitumor</subject><subject>Gene expression</subject><subject>Gene regulation</subject><subject>Genes</subject><subject>Humans</subject><subject>Oxidation</subject><subject>Peptides</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Peptides - pharmacology</subject><subject>Peroxiredoxin</subject><subject>peroxiredoxin-5</subject><subject>Peroxiredoxins - chemistry</subject><subject>Protein Conformation</subject><subject>Sequence Alignment</subject><subject>Structure-function relationships</subject><subject>transcriptome analysis</subject><subject>Transcriptomes</subject><subject>Tumorigenesis</subject><issn>1860-7179</issn><issn>1860-7187</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLw0AUhQdRbK1uXUrAjZvUeSYzy5L6gooudD0kkxtISTJ1Jqn23zultYIbN_fFdw-Hg9AlwVOCMb01bWmmFNOwMMqO0JjIBMcpkenxYU7VCJ15v8SYc0nkKRoxzgjDBI9RNq-9sWtwm8hW0azr635orYtmpq_XEL3Cqq9L8NEcXNjLqHK2DVdnv2oHZahdJM7RSZU3Hi72fYLe7-_essd48fLwlM0WsWEpY7HKJS-DgYokVBAFkvASSyoUh0IUXKWMU5kkrCB5ySAARhlmgEKRCMOqik3QzU535ezHAL7XbTAPTZN3YAevqRAi4VhJGtDrP-jSDq4L7gKlpCICCxGo6Y4yznrvoNIrV7e522iC9TZevY1XH-IND1d72aFooTzgP3kGQO2Az7qBzT9yOnueZ7_i33KahHM</recordid><startdate>20211119</startdate><enddate>20211119</enddate><creator>Liu, Juanjuan</creator><creator>Zou, Sen</creator><creator>Zhang, Yan</creator><creator>Lin, Ru</creator><creator>Duan, Yanbo</creator><creator>He, Weiqing</creator><creator>Yang, Zhaoyong</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></search><sort><creationdate>20211119</creationdate><title>Discovery of Antitumor Active Peptides Derived from Peroxiredoxin 5</title><author>Liu, Juanjuan ; Zou, Sen ; Zhang, Yan ; Lin, Ru ; Duan, Yanbo ; He, Weiqing ; Yang, Zhaoyong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3733-9a84d481f162519e814d082594eb5b4973428663b1ad3e19ec9c3ce2eb65c3ff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Amino Acid Sequence</topic><topic>Anticancer properties</topic><topic>Antineoplastic Agents - chemical synthesis</topic><topic>Antineoplastic Agents - chemistry</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>antioxidation</topic><topic>Antitumor activity</topic><topic>antitumor agents</topic><topic>Cell Line, Tumor</topic><topic>Cell Proliferation - drug effects</topic><topic>Cell Survival - drug effects</topic><topic>Crystal structure</topic><topic>Drug Screening Assays, Antitumor</topic><topic>Gene expression</topic><topic>Gene regulation</topic><topic>Genes</topic><topic>Humans</topic><topic>Oxidation</topic><topic>Peptides</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Peptides - pharmacology</topic><topic>Peroxiredoxin</topic><topic>peroxiredoxin-5</topic><topic>Peroxiredoxins - chemistry</topic><topic>Protein Conformation</topic><topic>Sequence Alignment</topic><topic>Structure-function relationships</topic><topic>transcriptome analysis</topic><topic>Transcriptomes</topic><topic>Tumorigenesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Juanjuan</creatorcontrib><creatorcontrib>Zou, Sen</creatorcontrib><creatorcontrib>Zhang, Yan</creatorcontrib><creatorcontrib>Lin, Ru</creatorcontrib><creatorcontrib>Duan, Yanbo</creatorcontrib><creatorcontrib>He, Weiqing</creatorcontrib><creatorcontrib>Yang, Zhaoyong</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>Liu, Juanjuan</au><au>Zou, Sen</au><au>Zhang, Yan</au><au>Lin, Ru</au><au>Duan, Yanbo</au><au>He, Weiqing</au><au>Yang, Zhaoyong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Discovery of Antitumor Active Peptides Derived from Peroxiredoxin 5</atitle><jtitle>ChemMedChem</jtitle><addtitle>ChemMedChem</addtitle><date>2021-11-19</date><risdate>2021</risdate><volume>16</volume><issue>22</issue><spage>3477</spage><epage>3483</epage><pages>3477-3483</pages><issn>1860-7179</issn><eissn>1860-7187</eissn><abstract>The peroxiredoxin 5 (PRDX5) is a member of peroxiredoxins with antitumor activity. However, as a recombinant protein, PRDX5 is restricted in clinic due to high cost and keeping high dose in medication. The alternative way is to explore the antitumor active fragments of PRDX5 for potential of peptide drugs. According to the sequence, crystal structure and enzyme function of PRDX5, seven peptides were designed and named as IMB‐P1∼7. The peptide IMB‐P1 (AFTPGCSKTHLPGFVEQAEAL) containing critical residue C47 exhibited antitumor activity similar to PRDX5 in vivo. Transcriptome analysis showed peptide IMB‐P1 could make influence on expression of multiple genes involved in tumorigenesis and deterioration. Besides, an important discovery is the down‐regulation of oxidation‐related genes. In CT26 cells, IMB‐P1 carried similar antitumor activity with increasing ROS level to intact PRDX5. The results demonstrated that peptide IMB‐P1 with easier synthesis from PRDX5 may serve as a promising antitumor candidate.
Fully functional fragment: Seven peptides were designed in accordance with the sequence, crystal structure, and enzyme function of PRDX5. The peptide IMB‐P1 (AFTPGCSKTHLPGFVEQAEAL) containing the critical residue C47 was found to retain similar antitumor activity as that of intact PRDX5 protein in vivo and in vitro.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>34313010</pmid><doi>10.1002/cmdc.202100323</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Sequence Anticancer properties Antineoplastic Agents - chemical synthesis Antineoplastic Agents - chemistry Antineoplastic Agents - pharmacology antioxidation Antitumor activity antitumor agents Cell Line, Tumor Cell Proliferation - drug effects Cell Survival - drug effects Crystal structure Drug Screening Assays, Antitumor Gene expression Gene regulation Genes Humans Oxidation Peptides Peptides - chemical synthesis Peptides - chemistry Peptides - pharmacology Peroxiredoxin peroxiredoxin-5 Peroxiredoxins - chemistry Protein Conformation Sequence Alignment Structure-function relationships transcriptome analysis Transcriptomes Tumorigenesis |
| title | Discovery of Antitumor Active Peptides Derived from Peroxiredoxin 5 |
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