Chia (Salvia hispanica L.) Seeds Contain a Highly Stable Trypsin Inhibitor with Potential for Bacterial Management Alone or in Drug Combination Therapy with Oxacillin
The emergence of antibiotic resistance poses a serious and challenging threat to healthcare systems, making it imperative to discover novel therapeutic options. This work reports the isolation and characterization of a thermostable trypsin inhibitor from chia ( Salvia hispanica L.) seeds, with antib...
Gespeichert in:
| Veröffentlicht in: | Probiotics and antimicrobial proteins 2023-10, Vol.15 (5), p.1221-1233 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1233 |
|---|---|
| container_issue | 5 |
| container_start_page | 1221 |
| container_title | Probiotics and antimicrobial proteins |
| container_volume | 15 |
| creator | de Souza, Adson Ávila Lima, Adrianne Maia dede Oliveira BezerraSousa, Daniele Nogueira, Francisca Cristiane do Sacramento Neto, José Carlos Dias, Lucas Pinheiro Araújo, Nadine Monteiro Salgueiro Nagano, Celso Shiniti Júnior, Hélio Vitoriano Nobre da Silva, Cecília Rocha do Amaral Valente Sá, Lívia Gurgel de Andrade Neto, João Batista Barroso, Fátima Daiana Dias de Moraes, Maria Elisabete Amaral de Oliveira, Hermógenes David |
| description | The emergence of antibiotic resistance poses a serious and challenging threat to healthcare systems, making it imperative to discover novel therapeutic options. This work reports the isolation and characterization of a thermostable trypsin inhibitor from chia (
Salvia hispanica
L.) seeds, with antibacterial activity against
Staphylococcus aureus
sensitive and resistant to methicillin. The trypsin inhibitor
Sh
TI was purified from chia seeds through crude extract heat treatment, followed by affinity and reversed-phase chromatography. Tricine-SDS–PAGE revealed a single glycoprotein band of ~ 11 kDa under nonreducing conditions, confirmed by mass spectrometry analysis (11.558 kDa).
Sh
TI was remarkably stable under high temperatures (100 °C; 120 min) and a broad pH range (2–10; 30 min). Upon exposure to DTT (0.1 M; 120 min),
Sh
TI antitrypsin activity was partially lost (~ 38%), indicating the participation of disulfide bridges in its structure.
Sh
TI is a competitive inhibitor (
K
i
= 1.79 × 10
–8
M; IC
50
= 1.74 × 10
–8
M) that forms a 1:1 stoichiometry ratio for the
Sh
TI:trypsin complex.
Sh
TI displayed antibacterial activity alone (MICs range from 15.83 to 19.03 µM) and in combination with oxacillin (FICI range from 0.20 to 0.33) against strains of
S. aureus
, including methicillin-resistant strains. Overproduction of reactive oxygen species and plasma membrane pore formation are involved in the antibacterial action mode of
Sh
TI. Overall,
Sh
TI represents a novel candidate for use as a therapeutic agent for the bacterial management of
S. aureus
infections. |
| doi_str_mv | 10.1007/s12602-022-09979-5 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2705751789</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2862635099</sourcerecordid><originalsourceid>FETCH-LOGICAL-c429t-86141943c90f11f2468837c3dd4571d81cd19b9a9a8ceddff4adb2793ecb33e3</originalsourceid><addsrcrecordid>eNqFkc1u1DAUhSNEJUrLC7CyxKYsUvyT2PGyDD-tNKiVZvbWjeNMXHnsYHsK80I8Jy5BILGgC-v63vudY1mnql4TfEkwFu8SoRzTGtNypBSybp9Vp6TjoiaMNM__3DF_Ub1M6R5jzhnFp9WP1WQBXWzAPZQ62TSDtxrQ-vIt2hgzJLQKPoP1CNC13U3uiDYZemfQNh7nVOY3frK9zSGibzZP6C5k47MFh8Yyeg86m_jYfQEPO7MvO3TlgjeobIv6QzzsyhP73nrINni0nUyE-biY3X4HbZ2z_rw6GcEl8-p3Pau2nz5uV9f1-vbzzepqXeuGylx3nDRENkxLPBIy0oZ3HROaDUPTCjJ0RA9E9hIkdNoMwzg2MPRUSGZ0z5hhZ9XFYjvH8PVgUlZ7m7RxDrwJh6QYaRmRBAv8JEoFbkVLRCcL-uYf9D4coi__ULTjlLO2ZFYoulA6hpSiGdUc7R7iURGsHkNWS8iqhKx-hazaImKLKBXY70z8a_0f1U-dpqq4</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2862635099</pqid></control><display><type>article</type><title>Chia (Salvia hispanica L.) Seeds Contain a Highly Stable Trypsin Inhibitor with Potential for Bacterial Management Alone or in Drug Combination Therapy with Oxacillin</title><source>SpringerLink Journals - AutoHoldings</source><creator>de Souza, Adson Ávila ; Lima, Adrianne Maia ; dede Oliveira BezerraSousa, Daniele ; Nogueira, Francisca Cristiane ; do Sacramento Neto, José Carlos ; Dias, Lucas Pinheiro ; Araújo, Nadine Monteiro Salgueiro ; Nagano, Celso Shiniti ; Júnior, Hélio Vitoriano Nobre ; da Silva, Cecília Rocha ; do Amaral Valente Sá, Lívia Gurgel ; de Andrade Neto, João Batista ; Barroso, Fátima Daiana Dias ; de Moraes, Maria Elisabete Amaral ; de Oliveira, Hermógenes David</creator><creatorcontrib>de Souza, Adson Ávila ; Lima, Adrianne Maia ; dede Oliveira BezerraSousa, Daniele ; Nogueira, Francisca Cristiane ; do Sacramento Neto, José Carlos ; Dias, Lucas Pinheiro ; Araújo, Nadine Monteiro Salgueiro ; Nagano, Celso Shiniti ; Júnior, Hélio Vitoriano Nobre ; da Silva, Cecília Rocha ; do Amaral Valente Sá, Lívia Gurgel ; de Andrade Neto, João Batista ; Barroso, Fátima Daiana Dias ; de Moraes, Maria Elisabete Amaral ; de Oliveira, Hermógenes David</creatorcontrib><description>The emergence of antibiotic resistance poses a serious and challenging threat to healthcare systems, making it imperative to discover novel therapeutic options. This work reports the isolation and characterization of a thermostable trypsin inhibitor from chia (
Salvia hispanica
L.) seeds, with antibacterial activity against
Staphylococcus aureus
sensitive and resistant to methicillin. The trypsin inhibitor
Sh
TI was purified from chia seeds through crude extract heat treatment, followed by affinity and reversed-phase chromatography. Tricine-SDS–PAGE revealed a single glycoprotein band of ~ 11 kDa under nonreducing conditions, confirmed by mass spectrometry analysis (11.558 kDa).
Sh
TI was remarkably stable under high temperatures (100 °C; 120 min) and a broad pH range (2–10; 30 min). Upon exposure to DTT (0.1 M; 120 min),
Sh
TI antitrypsin activity was partially lost (~ 38%), indicating the participation of disulfide bridges in its structure.
Sh
TI is a competitive inhibitor (
K
i
= 1.79 × 10
–8
M; IC
50
= 1.74 × 10
–8
M) that forms a 1:1 stoichiometry ratio for the
Sh
TI:trypsin complex.
Sh
TI displayed antibacterial activity alone (MICs range from 15.83 to 19.03 µM) and in combination with oxacillin (FICI range from 0.20 to 0.33) against strains of
S. aureus
, including methicillin-resistant strains. Overproduction of reactive oxygen species and plasma membrane pore formation are involved in the antibacterial action mode of
Sh
TI. Overall,
Sh
TI represents a novel candidate for use as a therapeutic agent for the bacterial management of
S. aureus
infections.</description><identifier>ISSN: 1867-1306</identifier><identifier>EISSN: 1867-1314</identifier><identifier>DOI: 10.1007/s12602-022-09979-5</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Antibacterial activity ; antibacterial properties ; Antibiotic resistance ; Antibiotics ; Antimicrobial agents ; Applied Microbiology ; Biomedical and Life Sciences ; Chemistry/Food Science ; Chromatography ; disulfides ; Dithiothreitol ; Drug resistance ; glycoproteins ; health services ; Heat resistance ; heat treatment ; Heat treatments ; High temperature ; Life Sciences ; mass spectrometry ; Mass spectroscopy ; Methicillin ; Microbiology ; Nutrition ; Oxacillin ; Peptides ; plasma membrane ; Probiotics ; Protein Science ; Proteins ; Reactive oxygen species ; reversed-phase liquid chromatography ; Salvia columbariae ; Salvia hispanica ; Seeds ; Staphylococcus aureus ; Stoichiometry ; Strains (organisms) ; therapeutics ; thermal stability ; Trypsin ; trypsin inhibitors</subject><ispartof>Probiotics and antimicrobial proteins, 2023-10, Vol.15 (5), p.1221-1233</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022. Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c429t-86141943c90f11f2468837c3dd4571d81cd19b9a9a8ceddff4adb2793ecb33e3</citedby><cites>FETCH-LOGICAL-c429t-86141943c90f11f2468837c3dd4571d81cd19b9a9a8ceddff4adb2793ecb33e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12602-022-09979-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12602-022-09979-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids></links><search><creatorcontrib>de Souza, Adson Ávila</creatorcontrib><creatorcontrib>Lima, Adrianne Maia</creatorcontrib><creatorcontrib>dede Oliveira BezerraSousa, Daniele</creatorcontrib><creatorcontrib>Nogueira, Francisca Cristiane</creatorcontrib><creatorcontrib>do Sacramento Neto, José Carlos</creatorcontrib><creatorcontrib>Dias, Lucas Pinheiro</creatorcontrib><creatorcontrib>Araújo, Nadine Monteiro Salgueiro</creatorcontrib><creatorcontrib>Nagano, Celso Shiniti</creatorcontrib><creatorcontrib>Júnior, Hélio Vitoriano Nobre</creatorcontrib><creatorcontrib>da Silva, Cecília Rocha</creatorcontrib><creatorcontrib>do Amaral Valente Sá, Lívia Gurgel</creatorcontrib><creatorcontrib>de Andrade Neto, João Batista</creatorcontrib><creatorcontrib>Barroso, Fátima Daiana Dias</creatorcontrib><creatorcontrib>de Moraes, Maria Elisabete Amaral</creatorcontrib><creatorcontrib>de Oliveira, Hermógenes David</creatorcontrib><title>Chia (Salvia hispanica L.) Seeds Contain a Highly Stable Trypsin Inhibitor with Potential for Bacterial Management Alone or in Drug Combination Therapy with Oxacillin</title><title>Probiotics and antimicrobial proteins</title><addtitle>Probiotics & Antimicro. Prot</addtitle><description>The emergence of antibiotic resistance poses a serious and challenging threat to healthcare systems, making it imperative to discover novel therapeutic options. This work reports the isolation and characterization of a thermostable trypsin inhibitor from chia (
Salvia hispanica
L.) seeds, with antibacterial activity against
Staphylococcus aureus
sensitive and resistant to methicillin. The trypsin inhibitor
Sh
TI was purified from chia seeds through crude extract heat treatment, followed by affinity and reversed-phase chromatography. Tricine-SDS–PAGE revealed a single glycoprotein band of ~ 11 kDa under nonreducing conditions, confirmed by mass spectrometry analysis (11.558 kDa).
Sh
TI was remarkably stable under high temperatures (100 °C; 120 min) and a broad pH range (2–10; 30 min). Upon exposure to DTT (0.1 M; 120 min),
Sh
TI antitrypsin activity was partially lost (~ 38%), indicating the participation of disulfide bridges in its structure.
Sh
TI is a competitive inhibitor (
K
i
= 1.79 × 10
–8
M; IC
50
= 1.74 × 10
–8
M) that forms a 1:1 stoichiometry ratio for the
Sh
TI:trypsin complex.
Sh
TI displayed antibacterial activity alone (MICs range from 15.83 to 19.03 µM) and in combination with oxacillin (FICI range from 0.20 to 0.33) against strains of
S. aureus
, including methicillin-resistant strains. Overproduction of reactive oxygen species and plasma membrane pore formation are involved in the antibacterial action mode of
Sh
TI. Overall,
Sh
TI represents a novel candidate for use as a therapeutic agent for the bacterial management of
S. aureus
infections.</description><subject>Antibacterial activity</subject><subject>antibacterial properties</subject><subject>Antibiotic resistance</subject><subject>Antibiotics</subject><subject>Antimicrobial agents</subject><subject>Applied Microbiology</subject><subject>Biomedical and Life Sciences</subject><subject>Chemistry/Food Science</subject><subject>Chromatography</subject><subject>disulfides</subject><subject>Dithiothreitol</subject><subject>Drug resistance</subject><subject>glycoproteins</subject><subject>health services</subject><subject>Heat resistance</subject><subject>heat treatment</subject><subject>Heat treatments</subject><subject>High temperature</subject><subject>Life Sciences</subject><subject>mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Methicillin</subject><subject>Microbiology</subject><subject>Nutrition</subject><subject>Oxacillin</subject><subject>Peptides</subject><subject>plasma membrane</subject><subject>Probiotics</subject><subject>Protein Science</subject><subject>Proteins</subject><subject>Reactive oxygen species</subject><subject>reversed-phase liquid chromatography</subject><subject>Salvia columbariae</subject><subject>Salvia hispanica</subject><subject>Seeds</subject><subject>Staphylococcus aureus</subject><subject>Stoichiometry</subject><subject>Strains (organisms)</subject><subject>therapeutics</subject><subject>thermal stability</subject><subject>Trypsin</subject><subject>trypsin inhibitors</subject><issn>1867-1306</issn><issn>1867-1314</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNqFkc1u1DAUhSNEJUrLC7CyxKYsUvyT2PGyDD-tNKiVZvbWjeNMXHnsYHsK80I8Jy5BILGgC-v63vudY1mnql4TfEkwFu8SoRzTGtNypBSybp9Vp6TjoiaMNM__3DF_Ub1M6R5jzhnFp9WP1WQBXWzAPZQ62TSDtxrQ-vIt2hgzJLQKPoP1CNC13U3uiDYZemfQNh7nVOY3frK9zSGibzZP6C5k47MFh8Yyeg86m_jYfQEPO7MvO3TlgjeobIv6QzzsyhP73nrINni0nUyE-biY3X4HbZ2z_rw6GcEl8-p3Pau2nz5uV9f1-vbzzepqXeuGylx3nDRENkxLPBIy0oZ3HROaDUPTCjJ0RA9E9hIkdNoMwzg2MPRUSGZ0z5hhZ9XFYjvH8PVgUlZ7m7RxDrwJh6QYaRmRBAv8JEoFbkVLRCcL-uYf9D4coi__ULTjlLO2ZFYoulA6hpSiGdUc7R7iURGsHkNWS8iqhKx-hazaImKLKBXY70z8a_0f1U-dpqq4</recordid><startdate>20231001</startdate><enddate>20231001</enddate><creator>de Souza, Adson Ávila</creator><creator>Lima, Adrianne Maia</creator><creator>dede Oliveira BezerraSousa, Daniele</creator><creator>Nogueira, Francisca Cristiane</creator><creator>do Sacramento Neto, José Carlos</creator><creator>Dias, Lucas Pinheiro</creator><creator>Araújo, Nadine Monteiro Salgueiro</creator><creator>Nagano, Celso Shiniti</creator><creator>Júnior, Hélio Vitoriano Nobre</creator><creator>da Silva, Cecília Rocha</creator><creator>do Amaral Valente Sá, Lívia Gurgel</creator><creator>de Andrade Neto, João Batista</creator><creator>Barroso, Fátima Daiana Dias</creator><creator>de Moraes, Maria Elisabete Amaral</creator><creator>de Oliveira, Hermógenes David</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>8FE</scope><scope>8FH</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope></search><sort><creationdate>20231001</creationdate><title>Chia (Salvia hispanica L.) Seeds Contain a Highly Stable Trypsin Inhibitor with Potential for Bacterial Management Alone or in Drug Combination Therapy with Oxacillin</title><author>de Souza, Adson Ávila ; Lima, Adrianne Maia ; dede Oliveira BezerraSousa, Daniele ; Nogueira, Francisca Cristiane ; do Sacramento Neto, José Carlos ; Dias, Lucas Pinheiro ; Araújo, Nadine Monteiro Salgueiro ; Nagano, Celso Shiniti ; Júnior, Hélio Vitoriano Nobre ; da Silva, Cecília Rocha ; do Amaral Valente Sá, Lívia Gurgel ; de Andrade Neto, João Batista ; Barroso, Fátima Daiana Dias ; de Moraes, Maria Elisabete Amaral ; de Oliveira, Hermógenes David</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c429t-86141943c90f11f2468837c3dd4571d81cd19b9a9a8ceddff4adb2793ecb33e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Antibacterial activity</topic><topic>antibacterial properties</topic><topic>Antibiotic resistance</topic><topic>Antibiotics</topic><topic>Antimicrobial agents</topic><topic>Applied Microbiology</topic><topic>Biomedical and Life Sciences</topic><topic>Chemistry/Food Science</topic><topic>Chromatography</topic><topic>disulfides</topic><topic>Dithiothreitol</topic><topic>Drug resistance</topic><topic>glycoproteins</topic><topic>health services</topic><topic>Heat resistance</topic><topic>heat treatment</topic><topic>Heat treatments</topic><topic>High temperature</topic><topic>Life Sciences</topic><topic>mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Methicillin</topic><topic>Microbiology</topic><topic>Nutrition</topic><topic>Oxacillin</topic><topic>Peptides</topic><topic>plasma membrane</topic><topic>Probiotics</topic><topic>Protein Science</topic><topic>Proteins</topic><topic>Reactive oxygen species</topic><topic>reversed-phase liquid chromatography</topic><topic>Salvia columbariae</topic><topic>Salvia hispanica</topic><topic>Seeds</topic><topic>Staphylococcus aureus</topic><topic>Stoichiometry</topic><topic>Strains (organisms)</topic><topic>therapeutics</topic><topic>thermal stability</topic><topic>Trypsin</topic><topic>trypsin inhibitors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>de Souza, Adson Ávila</creatorcontrib><creatorcontrib>Lima, Adrianne Maia</creatorcontrib><creatorcontrib>dede Oliveira BezerraSousa, Daniele</creatorcontrib><creatorcontrib>Nogueira, Francisca Cristiane</creatorcontrib><creatorcontrib>do Sacramento Neto, José Carlos</creatorcontrib><creatorcontrib>Dias, Lucas Pinheiro</creatorcontrib><creatorcontrib>Araújo, Nadine Monteiro Salgueiro</creatorcontrib><creatorcontrib>Nagano, Celso Shiniti</creatorcontrib><creatorcontrib>Júnior, Hélio Vitoriano Nobre</creatorcontrib><creatorcontrib>da Silva, Cecília Rocha</creatorcontrib><creatorcontrib>do Amaral Valente Sá, Lívia Gurgel</creatorcontrib><creatorcontrib>de Andrade Neto, João Batista</creatorcontrib><creatorcontrib>Barroso, Fátima Daiana Dias</creatorcontrib><creatorcontrib>de Moraes, Maria Elisabete Amaral</creatorcontrib><creatorcontrib>de Oliveira, Hermógenes David</creatorcontrib><collection>CrossRef</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Biological Science 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>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Probiotics and antimicrobial proteins</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>de Souza, Adson Ávila</au><au>Lima, Adrianne Maia</au><au>dede Oliveira BezerraSousa, Daniele</au><au>Nogueira, Francisca Cristiane</au><au>do Sacramento Neto, José Carlos</au><au>Dias, Lucas Pinheiro</au><au>Araújo, Nadine Monteiro Salgueiro</au><au>Nagano, Celso Shiniti</au><au>Júnior, Hélio Vitoriano Nobre</au><au>da Silva, Cecília Rocha</au><au>do Amaral Valente Sá, Lívia Gurgel</au><au>de Andrade Neto, João Batista</au><au>Barroso, Fátima Daiana Dias</au><au>de Moraes, Maria Elisabete Amaral</au><au>de Oliveira, Hermógenes David</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chia (Salvia hispanica L.) Seeds Contain a Highly Stable Trypsin Inhibitor with Potential for Bacterial Management Alone or in Drug Combination Therapy with Oxacillin</atitle><jtitle>Probiotics and antimicrobial proteins</jtitle><stitle>Probiotics & Antimicro. Prot</stitle><date>2023-10-01</date><risdate>2023</risdate><volume>15</volume><issue>5</issue><spage>1221</spage><epage>1233</epage><pages>1221-1233</pages><issn>1867-1306</issn><eissn>1867-1314</eissn><abstract>The emergence of antibiotic resistance poses a serious and challenging threat to healthcare systems, making it imperative to discover novel therapeutic options. This work reports the isolation and characterization of a thermostable trypsin inhibitor from chia (
Salvia hispanica
L.) seeds, with antibacterial activity against
Staphylococcus aureus
sensitive and resistant to methicillin. The trypsin inhibitor
Sh
TI was purified from chia seeds through crude extract heat treatment, followed by affinity and reversed-phase chromatography. Tricine-SDS–PAGE revealed a single glycoprotein band of ~ 11 kDa under nonreducing conditions, confirmed by mass spectrometry analysis (11.558 kDa).
Sh
TI was remarkably stable under high temperatures (100 °C; 120 min) and a broad pH range (2–10; 30 min). Upon exposure to DTT (0.1 M; 120 min),
Sh
TI antitrypsin activity was partially lost (~ 38%), indicating the participation of disulfide bridges in its structure.
Sh
TI is a competitive inhibitor (
K
i
= 1.79 × 10
–8
M; IC
50
= 1.74 × 10
–8
M) that forms a 1:1 stoichiometry ratio for the
Sh
TI:trypsin complex.
Sh
TI displayed antibacterial activity alone (MICs range from 15.83 to 19.03 µM) and in combination with oxacillin (FICI range from 0.20 to 0.33) against strains of
S. aureus
, including methicillin-resistant strains. Overproduction of reactive oxygen species and plasma membrane pore formation are involved in the antibacterial action mode of
Sh
TI. Overall,
Sh
TI represents a novel candidate for use as a therapeutic agent for the bacterial management of
S. aureus
infections.</abstract><cop>New York</cop><pub>Springer US</pub><doi>10.1007/s12602-022-09979-5</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1867-1306 |
| ispartof | Probiotics and antimicrobial proteins, 2023-10, Vol.15 (5), p.1221-1233 |
| issn | 1867-1306 1867-1314 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2705751789 |
| source | SpringerLink Journals - AutoHoldings |
| subjects | Antibacterial activity antibacterial properties Antibiotic resistance Antibiotics Antimicrobial agents Applied Microbiology Biomedical and Life Sciences Chemistry/Food Science Chromatography disulfides Dithiothreitol Drug resistance glycoproteins health services Heat resistance heat treatment Heat treatments High temperature Life Sciences mass spectrometry Mass spectroscopy Methicillin Microbiology Nutrition Oxacillin Peptides plasma membrane Probiotics Protein Science Proteins Reactive oxygen species reversed-phase liquid chromatography Salvia columbariae Salvia hispanica Seeds Staphylococcus aureus Stoichiometry Strains (organisms) therapeutics thermal stability Trypsin trypsin inhibitors |
| title | Chia (Salvia hispanica L.) Seeds Contain a Highly Stable Trypsin Inhibitor with Potential for Bacterial Management Alone or in Drug Combination Therapy with Oxacillin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T20%3A25%3A44IST&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=Chia%20(Salvia%20hispanica%20L.)%20Seeds%20Contain%20a%20Highly%20Stable%20Trypsin%20Inhibitor%20with%20Potential%20for%20Bacterial%20Management%20Alone%20or%20in%20Drug%20Combination%20Therapy%20with%20Oxacillin&rft.jtitle=Probiotics%20and%20antimicrobial%20proteins&rft.au=de%20Souza,%20Adson%20%C3%81vila&rft.date=2023-10-01&rft.volume=15&rft.issue=5&rft.spage=1221&rft.epage=1233&rft.pages=1221-1233&rft.issn=1867-1306&rft.eissn=1867-1314&rft_id=info:doi/10.1007/s12602-022-09979-5&rft_dat=%3Cproquest_cross%3E2862635099%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2862635099&rft_id=info:pmid/&rfr_iscdi=true |