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Novel mitochondrial complex I-inhibiting peptides restrain NADH dehydrogenase activity
The emergence of drug-resistant fungal pathogens is becoming increasingly serious due to overuse of antifungals. Antimicrobial peptides have potent activity against a broad spectrum of pathogens, including fungi, and are considered a potential new class of antifungals. In this study, we examined the...
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| Published in: | Scientific reports 2019-09, Vol.9 (1), p.13694-12, Article 13694 |
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| cites | cdi_FETCH-LOGICAL-c511t-aa994852138c2a1455453444b91482d7e7e1af960d59663a4e20d2871aa469823 |
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| creator | Xue, Yao-Peng Kao, Mou-Chieh Lan, Chung-Yu |
| description | The emergence of drug-resistant fungal pathogens is becoming increasingly serious due to overuse of antifungals. Antimicrobial peptides have potent activity against a broad spectrum of pathogens, including fungi, and are considered a potential new class of antifungals. In this study, we examined the activities of the newly designed peptides P-113Du and P-113Tri, together with their parental peptide P-113, against the human fungal pathogen
Candida albicans
. The results showed that these peptides inhibit mitochondrial complex I, specifically NADH dehydrogenase, of the electron transport chain. Moreover, P-113Du and P-113Tri also block alternative NADH dehydrogenases. Currently, most inhibitors of the mitochondrial complex I are small molecules or artificially-designed antibodies. Here, we demonstrated novel functions of antimicrobial peptides in inhibiting the mitochondrial complex I of
C
.
albican
s, providing insight in the development of new antifungal agents. |
| doi_str_mv | 10.1038/s41598-019-50114-2 |
| format | article |
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Candida albicans
. The results showed that these peptides inhibit mitochondrial complex I, specifically NADH dehydrogenase, of the electron transport chain. Moreover, P-113Du and P-113Tri also block alternative NADH dehydrogenases. Currently, most inhibitors of the mitochondrial complex I are small molecules or artificially-designed antibodies. Here, we demonstrated novel functions of antimicrobial peptides in inhibiting the mitochondrial complex I of
C
.
albican
s, providing insight in the development of new antifungal agents.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-019-50114-2</identifier><identifier>PMID: 31548559</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/326/22/1292 ; 631/61 ; Antifungal agents ; Antifungal Agents - pharmacology ; Antimicrobial peptides ; Candida albicans ; Candida albicans - drug effects ; Candida albicans - metabolism ; Dehydrogenases ; Drug resistance ; Electron transport chain ; Electron Transport Complex I - antagonists & inhibitors ; Fungi ; Histatins - pharmacology ; Humanities and Social Sciences ; Microbial Sensitivity Tests ; Mitochondria ; Mitochondria - drug effects ; Mitochondria - metabolism ; multidisciplinary ; NADH ; NADH dehydrogenase ; NADH Dehydrogenase - metabolism ; NADH-ubiquinone oxidoreductase ; Pathogens ; Peptides ; Reactive Oxygen Species - metabolism ; Science ; Science (multidisciplinary)</subject><ispartof>Scientific reports, 2019-09, Vol.9 (1), p.13694-12, Article 13694</ispartof><rights>The Author(s) 2019</rights><rights>2019. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c511t-aa994852138c2a1455453444b91482d7e7e1af960d59663a4e20d2871aa469823</citedby><cites>FETCH-LOGICAL-c511t-aa994852138c2a1455453444b91482d7e7e1af960d59663a4e20d2871aa469823</cites><orcidid>0000-0003-2852-4482</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2296108236/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2296108236?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31548559$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xue, Yao-Peng</creatorcontrib><creatorcontrib>Kao, Mou-Chieh</creatorcontrib><creatorcontrib>Lan, Chung-Yu</creatorcontrib><title>Novel mitochondrial complex I-inhibiting peptides restrain NADH dehydrogenase activity</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>The emergence of drug-resistant fungal pathogens is becoming increasingly serious due to overuse of antifungals. Antimicrobial peptides have potent activity against a broad spectrum of pathogens, including fungi, and are considered a potential new class of antifungals. In this study, we examined the activities of the newly designed peptides P-113Du and P-113Tri, together with their parental peptide P-113, against the human fungal pathogen
Candida albicans
. The results showed that these peptides inhibit mitochondrial complex I, specifically NADH dehydrogenase, of the electron transport chain. Moreover, P-113Du and P-113Tri also block alternative NADH dehydrogenases. Currently, most inhibitors of the mitochondrial complex I are small molecules or artificially-designed antibodies. Here, we demonstrated novel functions of antimicrobial peptides in inhibiting the mitochondrial complex I of
C
.
albican
s, providing insight in the development of new antifungal agents.</description><subject>631/326/22/1292</subject><subject>631/61</subject><subject>Antifungal agents</subject><subject>Antifungal Agents - pharmacology</subject><subject>Antimicrobial peptides</subject><subject>Candida albicans</subject><subject>Candida albicans - drug effects</subject><subject>Candida albicans - metabolism</subject><subject>Dehydrogenases</subject><subject>Drug resistance</subject><subject>Electron transport chain</subject><subject>Electron Transport Complex I - antagonists & inhibitors</subject><subject>Fungi</subject><subject>Histatins - pharmacology</subject><subject>Humanities and Social Sciences</subject><subject>Microbial Sensitivity Tests</subject><subject>Mitochondria</subject><subject>Mitochondria - drug effects</subject><subject>Mitochondria - metabolism</subject><subject>multidisciplinary</subject><subject>NADH</subject><subject>NADH dehydrogenase</subject><subject>NADH Dehydrogenase - metabolism</subject><subject>NADH-ubiquinone oxidoreductase</subject><subject>Pathogens</subject><subject>Peptides</subject><subject>Reactive Oxygen Species - metabolism</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><recordid>eNp9kUtLxDAUhYMoKuofcCEFN26quWnSNhtBfA6IbtRtyLR3ZiJtUpPO4Px7Mw-fC7NJ4H459xwOIYdAT4Fm5VngIGSZUpCpoAA8ZRtkl1EuUpYxtvnjvUMOQnil8QgmOchtspOB4KUQcpe8PLgZNklreldNnK290U1SubZr8D0ZpMZOzND0xo6TDrve1BgSj6H32tjk4eLqLqlxMq-9G6PVARNd9WZm-vk-2RrpJuDB-t4jzzfXT5d36f3j7eDy4j6tBECfai1lNMIgKyumgQvBRcY5H0rgJasLLBD0SOa0FjLPM82R0ZqVBWjNc1mybI-cr3S76bDFukIbrTWq86bVfq6cNur3xJqJGruZygtRABVR4GQt4N3bNCZTrQkVNo226KZBMRYX57ksFujxH_TVTb2N8ZYU0OgnjxRbUZV3IXgcfZkBqhbNqVVzKjanls2pRYyjnzG-vnz2FIFsBYQ4smP037v_kf0AGVGjeQ</recordid><startdate>20190923</startdate><enddate>20190923</enddate><creator>Xue, Yao-Peng</creator><creator>Kao, Mou-Chieh</creator><creator>Lan, Chung-Yu</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-2852-4482</orcidid></search><sort><creationdate>20190923</creationdate><title>Novel mitochondrial complex I-inhibiting peptides restrain NADH dehydrogenase activity</title><author>Xue, Yao-Peng ; Kao, Mou-Chieh ; Lan, Chung-Yu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c511t-aa994852138c2a1455453444b91482d7e7e1af960d59663a4e20d2871aa469823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>631/326/22/1292</topic><topic>631/61</topic><topic>Antifungal agents</topic><topic>Antifungal Agents - pharmacology</topic><topic>Antimicrobial peptides</topic><topic>Candida albicans</topic><topic>Candida albicans - drug effects</topic><topic>Candida albicans - metabolism</topic><topic>Dehydrogenases</topic><topic>Drug resistance</topic><topic>Electron transport chain</topic><topic>Electron Transport Complex I - antagonists & inhibitors</topic><topic>Fungi</topic><topic>Histatins - pharmacology</topic><topic>Humanities and Social Sciences</topic><topic>Microbial Sensitivity Tests</topic><topic>Mitochondria</topic><topic>Mitochondria - drug effects</topic><topic>Mitochondria - metabolism</topic><topic>multidisciplinary</topic><topic>NADH</topic><topic>NADH dehydrogenase</topic><topic>NADH Dehydrogenase - metabolism</topic><topic>NADH-ubiquinone oxidoreductase</topic><topic>Pathogens</topic><topic>Peptides</topic><topic>Reactive Oxygen Species - metabolism</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xue, Yao-Peng</creatorcontrib><creatorcontrib>Kao, Mou-Chieh</creatorcontrib><creatorcontrib>Lan, Chung-Yu</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Science Journals</collection><collection>Biological Science Database</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>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xue, Yao-Peng</au><au>Kao, Mou-Chieh</au><au>Lan, Chung-Yu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel mitochondrial complex I-inhibiting peptides restrain NADH dehydrogenase activity</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2019-09-23</date><risdate>2019</risdate><volume>9</volume><issue>1</issue><spage>13694</spage><epage>12</epage><pages>13694-12</pages><artnum>13694</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>The emergence of drug-resistant fungal pathogens is becoming increasingly serious due to overuse of antifungals. Antimicrobial peptides have potent activity against a broad spectrum of pathogens, including fungi, and are considered a potential new class of antifungals. In this study, we examined the activities of the newly designed peptides P-113Du and P-113Tri, together with their parental peptide P-113, against the human fungal pathogen
Candida albicans
. The results showed that these peptides inhibit mitochondrial complex I, specifically NADH dehydrogenase, of the electron transport chain. Moreover, P-113Du and P-113Tri also block alternative NADH dehydrogenases. Currently, most inhibitors of the mitochondrial complex I are small molecules or artificially-designed antibodies. Here, we demonstrated novel functions of antimicrobial peptides in inhibiting the mitochondrial complex I of
C
.
albican
s, providing insight in the development of new antifungal agents.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>31548559</pmid><doi>10.1038/s41598-019-50114-2</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0003-2852-4482</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Scientific reports, 2019-09, Vol.9 (1), p.13694-12, Article 13694 |
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| language | eng |
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| source | Open Access: PubMed Central; Publicly Available Content Database; Free Full-Text Journals in Chemistry; Springer Nature - nature.com Journals - Fully Open Access |
| subjects | 631/326/22/1292 631/61 Antifungal agents Antifungal Agents - pharmacology Antimicrobial peptides Candida albicans Candida albicans - drug effects Candida albicans - metabolism Dehydrogenases Drug resistance Electron transport chain Electron Transport Complex I - antagonists & inhibitors Fungi Histatins - pharmacology Humanities and Social Sciences Microbial Sensitivity Tests Mitochondria Mitochondria - drug effects Mitochondria - metabolism multidisciplinary NADH NADH dehydrogenase NADH Dehydrogenase - metabolism NADH-ubiquinone oxidoreductase Pathogens Peptides Reactive Oxygen Species - metabolism Science Science (multidisciplinary) |
| title | Novel mitochondrial complex I-inhibiting peptides restrain NADH dehydrogenase activity |
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