Neutrophil elastase inhibitor purification strategy from cowpea seeds
Serine proteases and its inhibitors are involved in physiological process and its deregulation lead to various diseases like Chronic Obstructive Pulmonary Disease (COPD), pulmonary emphysema, skin diseases, atherosclerosis, coagulation diseases, cancer, inflammatory diseases, neuronal disorders and...
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| creator | Ferreira, Graziele Cristina Duran, Adriana Feliciano Alves da Silva, Flavia Ribeiro Santos Bomediano, Livia de Moraes Machado, Gabriel Capella Sasaki, Sergio Daishi |
| description | Serine proteases and its inhibitors are involved in physiological process and its deregulation lead to various diseases like Chronic Obstructive Pulmonary Disease (COPD), pulmonary emphysema, skin diseases, atherosclerosis, coagulation diseases, cancer, inflammatory diseases, neuronal disorders and other diseases. Serine protease inhibitors have been described in many species, as well as in plants, including cowpea beans (Vigna unguiculata (L.) Walp). Here, we purified and characterized a protease inhibitor, named VuEI (Vigna unguiculata elastase inhibitor), from Vigna unguiculata, with inhibitory activity against HNE (human neutrophil elastase) and chymotrypsin but has no inhibitory activity against trypsin and thrombin. VuEI was obtained by alkaline protein extraction followed by three different chromatographic steps in sequence. First, an ion exchange chromatography using Hitrap Q column was employed, followed by two reversed-phase chromatography using Source15RPC and ACE18 columns. The molecular mass of VuEI was estimated in 10.99 kDa by MALDI-TOF mass spectrometry. The dissociation constant (Ki) to HNE was 9 pM. These data indicate that VuEI is a potent inhibitor of human neutrophil elastase, besides to inhibit chymotrypsin. |
| doi_str_mv | 10.1371/journal.pone.0223713 |
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Serine protease inhibitors have been described in many species, as well as in plants, including cowpea beans (Vigna unguiculata (L.) Walp). Here, we purified and characterized a protease inhibitor, named VuEI (Vigna unguiculata elastase inhibitor), from Vigna unguiculata, with inhibitory activity against HNE (human neutrophil elastase) and chymotrypsin but has no inhibitory activity against trypsin and thrombin. VuEI was obtained by alkaline protein extraction followed by three different chromatographic steps in sequence. First, an ion exchange chromatography using Hitrap Q column was employed, followed by two reversed-phase chromatography using Source15RPC and ACE18 columns. The molecular mass of VuEI was estimated in 10.99 kDa by MALDI-TOF mass spectrometry. The dissociation constant (Ki) to HNE was 9 pM. These data indicate that VuEI is a potent inhibitor of human neutrophil elastase, besides to inhibit chymotrypsin.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0223713</identifier><identifier>PMID: 31600323</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino acids ; Animals ; Arteriosclerosis ; Atherosclerosis ; Beans ; Biological Assay ; Biology and Life Sciences ; Cattle ; Chemical bonds ; Chromatography ; Chronic obstructive lung disease ; Chronic obstructive pulmonary disease ; Chymotrypsin ; Coagulation ; Column chromatography ; Cowpeas ; Deregulation ; Dissociation ; Drug therapy ; Elastase ; Emphysema ; Enzymes ; Hydrolases ; Inflammatory diseases ; Ion exchange ; Ion exchanging ; Legumes ; Leukocyte Elastase - isolation & purification ; Lung diseases ; Mass spectrometry ; Mass spectroscopy ; Medicine and Health Sciences ; Neurons ; Neutrophils ; Obstructive lung disease ; Plant Extracts - chemistry ; Protease ; Protease inhibitors ; Proteases ; Proteinase inhibitors ; Proteins ; Research and Analysis Methods ; Seeds ; Seeds - chemistry ; Serine ; Serine proteinase ; Serine Proteinase Inhibitors - isolation & purification ; Skin ; Skin diseases ; Soybeans ; Spectroscopy ; Thrombin ; Trypsin ; Vigna - chemistry ; Vigna unguiculata</subject><ispartof>PloS one, 2019-10, Vol.14 (10), p.e0223713-e0223713</ispartof><rights>COPYRIGHT 2019 Public Library of Science</rights><rights>2019 Ferreira et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://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. 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Serine protease inhibitors have been described in many species, as well as in plants, including cowpea beans (Vigna unguiculata (L.) Walp). Here, we purified and characterized a protease inhibitor, named VuEI (Vigna unguiculata elastase inhibitor), from Vigna unguiculata, with inhibitory activity against HNE (human neutrophil elastase) and chymotrypsin but has no inhibitory activity against trypsin and thrombin. VuEI was obtained by alkaline protein extraction followed by three different chromatographic steps in sequence. First, an ion exchange chromatography using Hitrap Q column was employed, followed by two reversed-phase chromatography using Source15RPC and ACE18 columns. The molecular mass of VuEI was estimated in 10.99 kDa by MALDI-TOF mass spectrometry. The dissociation constant (Ki) to HNE was 9 pM. These data indicate that VuEI is a potent inhibitor of human neutrophil elastase, besides to inhibit chymotrypsin.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Arteriosclerosis</subject><subject>Atherosclerosis</subject><subject>Beans</subject><subject>Biological Assay</subject><subject>Biology and Life Sciences</subject><subject>Cattle</subject><subject>Chemical bonds</subject><subject>Chromatography</subject><subject>Chronic obstructive lung disease</subject><subject>Chronic obstructive pulmonary disease</subject><subject>Chymotrypsin</subject><subject>Coagulation</subject><subject>Column chromatography</subject><subject>Cowpeas</subject><subject>Deregulation</subject><subject>Dissociation</subject><subject>Drug therapy</subject><subject>Elastase</subject><subject>Emphysema</subject><subject>Enzymes</subject><subject>Hydrolases</subject><subject>Inflammatory diseases</subject><subject>Ion exchange</subject><subject>Ion exchanging</subject><subject>Legumes</subject><subject>Leukocyte Elastase - isolation & purification</subject><subject>Lung diseases</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Medicine and Health Sciences</subject><subject>Neurons</subject><subject>Neutrophils</subject><subject>Obstructive lung disease</subject><subject>Plant Extracts - chemistry</subject><subject>Protease</subject><subject>Protease inhibitors</subject><subject>Proteases</subject><subject>Proteinase inhibitors</subject><subject>Proteins</subject><subject>Research and Analysis Methods</subject><subject>Seeds</subject><subject>Seeds - chemistry</subject><subject>Serine</subject><subject>Serine proteinase</subject><subject>Serine Proteinase Inhibitors - isolation & purification</subject><subject>Skin</subject><subject>Skin diseases</subject><subject>Soybeans</subject><subject>Spectroscopy</subject><subject>Thrombin</subject><subject>Trypsin</subject><subject>Vigna - 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elastase inhibitor purification strategy from cowpea seeds</title><author>Ferreira, Graziele Cristina ; Duran, Adriana Feliciano Alves ; da Silva, Flavia Ribeiro Santos ; Bomediano, Livia de Moraes ; Machado, Gabriel Capella ; Sasaki, Sergio Daishi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-c34476c7d9aa955d6996aee50a2c272db3091ab954515bea0bdf7d578c20f9a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Amino acids</topic><topic>Animals</topic><topic>Arteriosclerosis</topic><topic>Atherosclerosis</topic><topic>Beans</topic><topic>Biological Assay</topic><topic>Biology and Life Sciences</topic><topic>Cattle</topic><topic>Chemical bonds</topic><topic>Chromatography</topic><topic>Chronic obstructive lung disease</topic><topic>Chronic obstructive pulmonary disease</topic><topic>Chymotrypsin</topic><topic>Coagulation</topic><topic>Column chromatography</topic><topic>Cowpeas</topic><topic>Deregulation</topic><topic>Dissociation</topic><topic>Drug therapy</topic><topic>Elastase</topic><topic>Emphysema</topic><topic>Enzymes</topic><topic>Hydrolases</topic><topic>Inflammatory diseases</topic><topic>Ion exchange</topic><topic>Ion exchanging</topic><topic>Legumes</topic><topic>Leukocyte Elastase - isolation & purification</topic><topic>Lung diseases</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Medicine and Health Sciences</topic><topic>Neurons</topic><topic>Neutrophils</topic><topic>Obstructive lung disease</topic><topic>Plant Extracts - chemistry</topic><topic>Protease</topic><topic>Protease inhibitors</topic><topic>Proteases</topic><topic>Proteinase inhibitors</topic><topic>Proteins</topic><topic>Research and Analysis Methods</topic><topic>Seeds</topic><topic>Seeds - chemistry</topic><topic>Serine</topic><topic>Serine proteinase</topic><topic>Serine Proteinase Inhibitors - isolation & 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One</addtitle><date>2019-10-10</date><risdate>2019</risdate><volume>14</volume><issue>10</issue><spage>e0223713</spage><epage>e0223713</epage><pages>e0223713-e0223713</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Serine proteases and its inhibitors are involved in physiological process and its deregulation lead to various diseases like Chronic Obstructive Pulmonary Disease (COPD), pulmonary emphysema, skin diseases, atherosclerosis, coagulation diseases, cancer, inflammatory diseases, neuronal disorders and other diseases. Serine protease inhibitors have been described in many species, as well as in plants, including cowpea beans (Vigna unguiculata (L.) Walp). Here, we purified and characterized a protease inhibitor, named VuEI (Vigna unguiculata elastase inhibitor), from Vigna unguiculata, with inhibitory activity against HNE (human neutrophil elastase) and chymotrypsin but has no inhibitory activity against trypsin and thrombin. VuEI was obtained by alkaline protein extraction followed by three different chromatographic steps in sequence. First, an ion exchange chromatography using Hitrap Q column was employed, followed by two reversed-phase chromatography using Source15RPC and ACE18 columns. The molecular mass of VuEI was estimated in 10.99 kDa by MALDI-TOF mass spectrometry. The dissociation constant (Ki) to HNE was 9 pM. These data indicate that VuEI is a potent inhibitor of human neutrophil elastase, besides to inhibit chymotrypsin.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>31600323</pmid><doi>10.1371/journal.pone.0223713</doi><tpages>e0223713</tpages><orcidid>https://orcid.org/0000-0002-6233-3316</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | PloS one, 2019-10, Vol.14 (10), p.e0223713-e0223713 |
| issn | 1932-6203 1932-6203 |
| language | eng |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Public Library of Science (PLoS); PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino acids Animals Arteriosclerosis Atherosclerosis Beans Biological Assay Biology and Life Sciences Cattle Chemical bonds Chromatography Chronic obstructive lung disease Chronic obstructive pulmonary disease Chymotrypsin Coagulation Column chromatography Cowpeas Deregulation Dissociation Drug therapy Elastase Emphysema Enzymes Hydrolases Inflammatory diseases Ion exchange Ion exchanging Legumes Leukocyte Elastase - isolation & purification Lung diseases Mass spectrometry Mass spectroscopy Medicine and Health Sciences Neurons Neutrophils Obstructive lung disease Plant Extracts - chemistry Protease Protease inhibitors Proteases Proteinase inhibitors Proteins Research and Analysis Methods Seeds Seeds - chemistry Serine Serine proteinase Serine Proteinase Inhibitors - isolation & purification Skin Skin diseases Soybeans Spectroscopy Thrombin Trypsin Vigna - chemistry Vigna unguiculata |
| title | Neutrophil elastase inhibitor purification strategy from cowpea seeds |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T14%3A07%3A06IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Neutrophil%20elastase%20inhibitor%20purification%20strategy%20from%20cowpea%20seeds&rft.jtitle=PloS%20one&rft.au=Ferreira,%20Graziele%20Cristina&rft.date=2019-10-10&rft.volume=14&rft.issue=10&rft.spage=e0223713&rft.epage=e0223713&rft.pages=e0223713-e0223713&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0223713&rft_dat=%3Cgale_plos_%3EA602311754%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2303979437&rft_id=info:pmid/31600323&rft_galeid=A602311754&rft_doaj_id=oai_doaj_org_article_49fc921d334149c79661bc4f077d3768&rfr_iscdi=true |