Structure based design and synthesis of peptide inhibitor of human LOX-12: in vitro and in vivo analysis of a novel therapeutic agent for breast cancer
Human breast cancer cell proliferation involves a complex interaction between growth factors, steroid hormones and peptide hormones. The interaction of growth factors, such as epidermal growth factor (EGF), with their receptors on breast cancer cells can lead to the hydrolysis of phospholipids and r...
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| Veröffentlicht in: | PloS one 2012-02, Vol.7 (2), p.e32521 |
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| description | Human breast cancer cell proliferation involves a complex interaction between growth factors, steroid hormones and peptide hormones. The interaction of growth factors, such as epidermal growth factor (EGF), with their receptors on breast cancer cells can lead to the hydrolysis of phospholipids and release of fatty acid such as arachidonic acid, which can be further metabolized by cyclooxygenase (COX) and lipoxygenase (LOX) pathways to produce prostaglandins. The high concentration of prostaglandins has been associated with chronic inflammatory diseases and several types of human cancers. This is due to the over expression COX, LOX and other inflammatory enzymes. Ten peptides were designed and synthesized by solid phase peptide synthesis and analyzed in vitro for enzyme inhibition. Out of these peptides, YWCS had shown significant inhibitory effects. The dissociation constant (K(D)) was determined by surface plasmon resonance (SPR) analysis and was found to be 3.39 × 10(-8) M and 8.6 × 10(-8) M for YWCS and baicalein (positive control), respectively. The kinetic constant Ki was 72.45 × 10(-7) M as determined by kinetic assay. The peptide significantly reduced the cell viability of estrogen positive MCF-7 and estrogen negative MDA-MB-231 cell line with the half maximal concentration (IC(50)) of 75 µM and 400 µM, respectively. The peptide also induced 49.8% and 20.8% apoptosis in breast cancer cells MCF-7 and MDA-MB-231, respectively. The YWCS was also found to be least hemolytic at a concentration of 358 µM. In vivo studies had shown that the peptide significantly inhibits tumor growth in mice (p |
| doi_str_mv | 10.1371/journal.pone.0032521 |
| format | Article |
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The interaction of growth factors, such as epidermal growth factor (EGF), with their receptors on breast cancer cells can lead to the hydrolysis of phospholipids and release of fatty acid such as arachidonic acid, which can be further metabolized by cyclooxygenase (COX) and lipoxygenase (LOX) pathways to produce prostaglandins. The high concentration of prostaglandins has been associated with chronic inflammatory diseases and several types of human cancers. This is due to the over expression COX, LOX and other inflammatory enzymes. Ten peptides were designed and synthesized by solid phase peptide synthesis and analyzed in vitro for enzyme inhibition. Out of these peptides, YWCS had shown significant inhibitory effects. The dissociation constant (K(D)) was determined by surface plasmon resonance (SPR) analysis and was found to be 3.39 × 10(-8) M and 8.6 × 10(-8) M for YWCS and baicalein (positive control), respectively. The kinetic constant Ki was 72.45 × 10(-7) M as determined by kinetic assay. The peptide significantly reduced the cell viability of estrogen positive MCF-7 and estrogen negative MDA-MB-231 cell line with the half maximal concentration (IC(50)) of 75 µM and 400 µM, respectively. The peptide also induced 49.8% and 20.8% apoptosis in breast cancer cells MCF-7 and MDA-MB-231, respectively. The YWCS was also found to be least hemolytic at a concentration of 358 µM. In vivo studies had shown that the peptide significantly inhibits tumor growth in mice (p<0.017). This peptide can be used as a lead compound and complement for ongoing efforts to develop differentiation therapies for breast cancer.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0032521</identifier><identifier>PMID: 22384268</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Animals ; Antineoplastic Agents - pharmacology ; Apoptosis ; Arachidonate 12-Lipoxygenase - chemistry ; Arachidonic acid ; Biochemistry ; Biology ; Biophysics ; Breast cancer ; Breast Neoplasms - drug therapy ; Breast Neoplasms - enzymology ; Cancer ; Cancer therapies ; Cell Line, Tumor ; Cell proliferation ; Cell Survival ; Chemical compounds ; Chemistry, Pharmaceutical - methods ; Chemotherapy ; Cloning ; Cytotoxicity ; Development and progression ; Dissociation ; Drug Design ; Drug Screening Assays, Antitumor ; Enzymes ; Epidermal growth factor ; Epidermal growth factors ; Estrogens ; Estrogens - metabolism ; Ethics ; Fatty acids ; Female ; Flow Cytometry - methods ; Glycine max ; Growth factors ; Health aspects ; Hormones ; Humans ; In vivo methods and tests ; Inflammatory diseases ; Inhibitory Concentration 50 ; Kinetics ; Laboratory animals ; Lipoxygenase ; Lipoxygenase Inhibitors - chemical synthesis ; Lipoxygenase Inhibitors - chemistry ; Liquid oxygen ; Mammary Neoplasms, Animal - drug therapy ; Mammary Neoplasms, Animal - enzymology ; Medicine ; Membrane lipids ; Metastasis ; Mice ; Pathogenesis ; Peptide hormones ; Peptide inhibitors ; Peptide synthesis ; Peptides ; Peptides - chemistry ; Pharmacology ; Phospholipids ; Prostaglandin endoperoxide synthase ; Prostaglandins ; Protein Binding ; Proteins ; Receptors ; Recombinant Proteins - metabolism ; Solvents ; Steroid hormones ; Studies ; Surface plasmon resonance ; Synthesis ; Unsaturated fatty acids</subject><ispartof>PloS one, 2012-02, Vol.7 (2), p.e32521</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>2012 Singh et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Singh et al. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c691t-6b039c39ff494b67ca6f8487fb5649894da8dc752e0f1c8086bed587a04de68d3</citedby><cites>FETCH-LOGICAL-c691t-6b039c39ff494b67ca6f8487fb5649894da8dc752e0f1c8086bed587a04de68d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3285689/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3285689/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22384268$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Khan, Rizwan Hasan</contributor><creatorcontrib>Singh, Abhay Kumar</creatorcontrib><creatorcontrib>Singh, Ratnakar</creatorcontrib><creatorcontrib>Naz, Farhat</creatorcontrib><creatorcontrib>Chauhan, Shyam Singh</creatorcontrib><creatorcontrib>Dinda, Amit</creatorcontrib><creatorcontrib>Shukla, Abhay Anand</creatorcontrib><creatorcontrib>Gill, Kamaldeep</creatorcontrib><creatorcontrib>Kapoor, Vaishali</creatorcontrib><creatorcontrib>Dey, Sharmistha</creatorcontrib><title>Structure based design and synthesis of peptide inhibitor of human LOX-12: in vitro and in vivo analysis of a novel therapeutic agent for breast cancer</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Human breast cancer cell proliferation involves a complex interaction between growth factors, steroid hormones and peptide hormones. The interaction of growth factors, such as epidermal growth factor (EGF), with their receptors on breast cancer cells can lead to the hydrolysis of phospholipids and release of fatty acid such as arachidonic acid, which can be further metabolized by cyclooxygenase (COX) and lipoxygenase (LOX) pathways to produce prostaglandins. The high concentration of prostaglandins has been associated with chronic inflammatory diseases and several types of human cancers. This is due to the over expression COX, LOX and other inflammatory enzymes. Ten peptides were designed and synthesized by solid phase peptide synthesis and analyzed in vitro for enzyme inhibition. Out of these peptides, YWCS had shown significant inhibitory effects. The dissociation constant (K(D)) was determined by surface plasmon resonance (SPR) analysis and was found to be 3.39 × 10(-8) M and 8.6 × 10(-8) M for YWCS and baicalein (positive control), respectively. The kinetic constant Ki was 72.45 × 10(-7) M as determined by kinetic assay. The peptide significantly reduced the cell viability of estrogen positive MCF-7 and estrogen negative MDA-MB-231 cell line with the half maximal concentration (IC(50)) of 75 µM and 400 µM, respectively. The peptide also induced 49.8% and 20.8% apoptosis in breast cancer cells MCF-7 and MDA-MB-231, respectively. The YWCS was also found to be least hemolytic at a concentration of 358 µM. In vivo studies had shown that the peptide significantly inhibits tumor growth in mice (p<0.017). This peptide can be used as a lead compound and complement for ongoing efforts to develop differentiation therapies for breast cancer.</description><subject>Animals</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Apoptosis</subject><subject>Arachidonate 12-Lipoxygenase - chemistry</subject><subject>Arachidonic acid</subject><subject>Biochemistry</subject><subject>Biology</subject><subject>Biophysics</subject><subject>Breast cancer</subject><subject>Breast Neoplasms - drug therapy</subject><subject>Breast Neoplasms - enzymology</subject><subject>Cancer</subject><subject>Cancer therapies</subject><subject>Cell Line, Tumor</subject><subject>Cell proliferation</subject><subject>Cell Survival</subject><subject>Chemical compounds</subject><subject>Chemistry, Pharmaceutical - methods</subject><subject>Chemotherapy</subject><subject>Cloning</subject><subject>Cytotoxicity</subject><subject>Development and progression</subject><subject>Dissociation</subject><subject>Drug Design</subject><subject>Drug Screening Assays, Antitumor</subject><subject>Enzymes</subject><subject>Epidermal growth factor</subject><subject>Epidermal growth factors</subject><subject>Estrogens</subject><subject>Estrogens - metabolism</subject><subject>Ethics</subject><subject>Fatty acids</subject><subject>Female</subject><subject>Flow Cytometry - methods</subject><subject>Glycine max</subject><subject>Growth factors</subject><subject>Health aspects</subject><subject>Hormones</subject><subject>Humans</subject><subject>In vivo methods and tests</subject><subject>Inflammatory diseases</subject><subject>Inhibitory Concentration 50</subject><subject>Kinetics</subject><subject>Laboratory animals</subject><subject>Lipoxygenase</subject><subject>Lipoxygenase Inhibitors - chemical synthesis</subject><subject>Lipoxygenase Inhibitors - chemistry</subject><subject>Liquid oxygen</subject><subject>Mammary Neoplasms, Animal - drug therapy</subject><subject>Mammary Neoplasms, Animal - enzymology</subject><subject>Medicine</subject><subject>Membrane lipids</subject><subject>Metastasis</subject><subject>Mice</subject><subject>Pathogenesis</subject><subject>Peptide hormones</subject><subject>Peptide inhibitors</subject><subject>Peptide synthesis</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Pharmacology</subject><subject>Phospholipids</subject><subject>Prostaglandin endoperoxide synthase</subject><subject>Prostaglandins</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Recombinant Proteins - metabolism</subject><subject>Solvents</subject><subject>Steroid hormones</subject><subject>Studies</subject><subject>Surface plasmon resonance</subject><subject>Synthesis</subject><subject>Unsaturated fatty acids</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNk9-KEzEUxgdR3HX1DUQDguBFazKZyWS8EJbFP4VCwVXxLpxJMm3KNBmTTLFP4uuatrNLCwoyF5Oc_L4vyUdOlj0neEpoRd6u3eAtdNPeWT3FmOZlTh5kl6Sm-YTlmD48GV9kT0JYY1xSztjj7CLPKS9yxi-z37fRDzIOXqMGglZI6WCWFoFVKOxsXKVpQK5Fve6jURoZuzKNic7vi6thAxbNFz8mJH-XltDWRO8O4sNkux9Dtxs9AFm31R1Krh56PUQjESy1jahNfo3XECKSYKX2T7NHLXRBPxv_V9m3jx--3nyezBefZjfX84lkNYkT1mBaS1q3bVEXDasksJYXvGqbkhU1rwsFXMmqzDVuieSYs0arkleAC6UZV_Qqe3n07TsXxJhpEISmhEqCMU_E7EgoB2vRe7MBvxMOjDgUnF8K8OkmnRbQQA0UWEEILrCquWqSA-ENhrJk1d7r_bjb0Gy0kunqHroz0_MVa1Zi6baC5rxkvE4Gr0YD734OOsR_HHmklpBOZWzrkpncmCDFdVFVuCRlSRM1_QuVPqU3RqZX1ZpUPxO8ORMkJupfcQlDCGJ2--X_2cX3c_b1CbvS0MVVcF16Hs6Gc7A4gtK7ELxu75MjWOyb4i4NsW8KMTZFkr04Tf1edNcF9A_96Agu</recordid><startdate>20120223</startdate><enddate>20120223</enddate><creator>Singh, Abhay Kumar</creator><creator>Singh, Ratnakar</creator><creator>Naz, Farhat</creator><creator>Chauhan, Shyam Singh</creator><creator>Dinda, Amit</creator><creator>Shukla, Abhay Anand</creator><creator>Gill, Kamaldeep</creator><creator>Kapoor, Vaishali</creator><creator>Dey, Sharmistha</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20120223</creationdate><title>Structure based design and synthesis of peptide inhibitor of human LOX-12: in vitro and in vivo analysis of a novel therapeutic agent for breast cancer</title><author>Singh, Abhay Kumar ; Singh, Ratnakar ; Naz, Farhat ; Chauhan, Shyam Singh ; Dinda, Amit ; Shukla, Abhay Anand ; Gill, Kamaldeep ; Kapoor, Vaishali ; Dey, Sharmistha</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c691t-6b039c39ff494b67ca6f8487fb5649894da8dc752e0f1c8086bed587a04de68d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animals</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Apoptosis</topic><topic>Arachidonate 12-Lipoxygenase - chemistry</topic><topic>Arachidonic acid</topic><topic>Biochemistry</topic><topic>Biology</topic><topic>Biophysics</topic><topic>Breast cancer</topic><topic>Breast Neoplasms - drug therapy</topic><topic>Breast Neoplasms - enzymology</topic><topic>Cancer</topic><topic>Cancer therapies</topic><topic>Cell Line, Tumor</topic><topic>Cell proliferation</topic><topic>Cell Survival</topic><topic>Chemical compounds</topic><topic>Chemistry, Pharmaceutical - methods</topic><topic>Chemotherapy</topic><topic>Cloning</topic><topic>Cytotoxicity</topic><topic>Development and progression</topic><topic>Dissociation</topic><topic>Drug Design</topic><topic>Drug Screening Assays, Antitumor</topic><topic>Enzymes</topic><topic>Epidermal growth factor</topic><topic>Epidermal growth factors</topic><topic>Estrogens</topic><topic>Estrogens - metabolism</topic><topic>Ethics</topic><topic>Fatty acids</topic><topic>Female</topic><topic>Flow Cytometry - methods</topic><topic>Glycine max</topic><topic>Growth factors</topic><topic>Health aspects</topic><topic>Hormones</topic><topic>Humans</topic><topic>In vivo methods and tests</topic><topic>Inflammatory diseases</topic><topic>Inhibitory Concentration 50</topic><topic>Kinetics</topic><topic>Laboratory animals</topic><topic>Lipoxygenase</topic><topic>Lipoxygenase Inhibitors - chemical synthesis</topic><topic>Lipoxygenase Inhibitors - chemistry</topic><topic>Liquid oxygen</topic><topic>Mammary Neoplasms, Animal - drug therapy</topic><topic>Mammary Neoplasms, Animal - enzymology</topic><topic>Medicine</topic><topic>Membrane lipids</topic><topic>Metastasis</topic><topic>Mice</topic><topic>Pathogenesis</topic><topic>Peptide hormones</topic><topic>Peptide inhibitors</topic><topic>Peptide synthesis</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Pharmacology</topic><topic>Phospholipids</topic><topic>Prostaglandin endoperoxide synthase</topic><topic>Prostaglandins</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Receptors</topic><topic>Recombinant Proteins - 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Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Singh, Abhay Kumar</au><au>Singh, Ratnakar</au><au>Naz, Farhat</au><au>Chauhan, Shyam Singh</au><au>Dinda, Amit</au><au>Shukla, Abhay Anand</au><au>Gill, Kamaldeep</au><au>Kapoor, Vaishali</au><au>Dey, Sharmistha</au><au>Khan, Rizwan Hasan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure based design and synthesis of peptide inhibitor of human LOX-12: in vitro and in vivo analysis of a novel therapeutic agent for breast cancer</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2012-02-23</date><risdate>2012</risdate><volume>7</volume><issue>2</issue><spage>e32521</spage><pages>e32521-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Human breast cancer cell proliferation involves a complex interaction between growth factors, steroid hormones and peptide hormones. The interaction of growth factors, such as epidermal growth factor (EGF), with their receptors on breast cancer cells can lead to the hydrolysis of phospholipids and release of fatty acid such as arachidonic acid, which can be further metabolized by cyclooxygenase (COX) and lipoxygenase (LOX) pathways to produce prostaglandins. The high concentration of prostaglandins has been associated with chronic inflammatory diseases and several types of human cancers. This is due to the over expression COX, LOX and other inflammatory enzymes. Ten peptides were designed and synthesized by solid phase peptide synthesis and analyzed in vitro for enzyme inhibition. Out of these peptides, YWCS had shown significant inhibitory effects. The dissociation constant (K(D)) was determined by surface plasmon resonance (SPR) analysis and was found to be 3.39 × 10(-8) M and 8.6 × 10(-8) M for YWCS and baicalein (positive control), respectively. The kinetic constant Ki was 72.45 × 10(-7) M as determined by kinetic assay. The peptide significantly reduced the cell viability of estrogen positive MCF-7 and estrogen negative MDA-MB-231 cell line with the half maximal concentration (IC(50)) of 75 µM and 400 µM, respectively. The peptide also induced 49.8% and 20.8% apoptosis in breast cancer cells MCF-7 and MDA-MB-231, respectively. The YWCS was also found to be least hemolytic at a concentration of 358 µM. In vivo studies had shown that the peptide significantly inhibits tumor growth in mice (p<0.017). This peptide can be used as a lead compound and complement for ongoing efforts to develop differentiation therapies for breast cancer.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22384268</pmid><doi>10.1371/journal.pone.0032521</doi><tpages>e32521</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2012-02, Vol.7 (2), p.e32521 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1323851008 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Animals Antineoplastic Agents - pharmacology Apoptosis Arachidonate 12-Lipoxygenase - chemistry Arachidonic acid Biochemistry Biology Biophysics Breast cancer Breast Neoplasms - drug therapy Breast Neoplasms - enzymology Cancer Cancer therapies Cell Line, Tumor Cell proliferation Cell Survival Chemical compounds Chemistry, Pharmaceutical - methods Chemotherapy Cloning Cytotoxicity Development and progression Dissociation Drug Design Drug Screening Assays, Antitumor Enzymes Epidermal growth factor Epidermal growth factors Estrogens Estrogens - metabolism Ethics Fatty acids Female Flow Cytometry - methods Glycine max Growth factors Health aspects Hormones Humans In vivo methods and tests Inflammatory diseases Inhibitory Concentration 50 Kinetics Laboratory animals Lipoxygenase Lipoxygenase Inhibitors - chemical synthesis Lipoxygenase Inhibitors - chemistry Liquid oxygen Mammary Neoplasms, Animal - drug therapy Mammary Neoplasms, Animal - enzymology Medicine Membrane lipids Metastasis Mice Pathogenesis Peptide hormones Peptide inhibitors Peptide synthesis Peptides Peptides - chemistry Pharmacology Phospholipids Prostaglandin endoperoxide synthase Prostaglandins Protein Binding Proteins Receptors Recombinant Proteins - metabolism Solvents Steroid hormones Studies Surface plasmon resonance Synthesis Unsaturated fatty acids |
| title | Structure based design and synthesis of peptide inhibitor of human LOX-12: in vitro and in vivo analysis of a novel therapeutic agent for breast cancer |
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