Bioactivity of melianone against Salmonella and in silico prediction of a membrane protein target
Melianone, the protolimonoid (24, 25-epoxyflindissone), was isolated from the medicinal tree species, Swietenia mahagoni (L.) JACQ (Meliaceae). The compound isolated from petroleum ether leaf extracts (5.39%) was quantified using high-performance thin-layer chromatography (HPTLC) method. In antimicr...
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| creator | Veni, A. Lokeswari, T. S. Krishna Kumari, G. N. Gayathri, D. Sudandiradoss, C. |
| description | Melianone, the protolimonoid (24, 25-epoxyflindissone), was isolated from the medicinal tree species,
Swietenia mahagoni
(L.) JACQ (Meliaceae). The compound isolated from petroleum ether leaf extracts (5.39%) was quantified using high-performance thin-layer chromatography (HPTLC) method. In antimicrobial assays melianone inhibited
Salmonella
ser
.
Typhi with an MIC of 0.053 µM. Induced Fit Docking (IFD) of the ligand, melianone, with proteins involved in anaerobic virulence of the pathogen, revealed that it binds with FocA (a transport protein of formate ions) at its “periplasmic opening” with a glide energy of − 51.8576 kcal mol
−1
. Melianone altered the overall conformation of the protein (protomer A) by 0.347 Å RMSD. It induced a notable protein topology (Ω loop region) shift in the channel from an intermediate-open to a closed-state conformation and was supported by molecular dynamic simulations performed. FocA, a protein that contributes to its survival under anaerobic conditions, was further evaluated experimentally, after exposure of
Salmonella
ser. Typhi to melianone, resulting in the altered homeostasis of formate. |
| doi_str_mv | 10.1007/s13205-020-02441-9 |
| format | Article |
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Swietenia mahagoni
(L.) JACQ (Meliaceae). The compound isolated from petroleum ether leaf extracts (5.39%) was quantified using high-performance thin-layer chromatography (HPTLC) method. In antimicrobial assays melianone inhibited
Salmonella
ser
.
Typhi with an MIC of 0.053 µM. Induced Fit Docking (IFD) of the ligand, melianone, with proteins involved in anaerobic virulence of the pathogen, revealed that it binds with FocA (a transport protein of formate ions) at its “periplasmic opening” with a glide energy of − 51.8576 kcal mol
−1
. Melianone altered the overall conformation of the protein (protomer A) by 0.347 Å RMSD. It induced a notable protein topology (Ω loop region) shift in the channel from an intermediate-open to a closed-state conformation and was supported by molecular dynamic simulations performed. FocA, a protein that contributes to its survival under anaerobic conditions, was further evaluated experimentally, after exposure of
Salmonella
ser. Typhi to melianone, resulting in the altered homeostasis of formate.</description><identifier>ISSN: 2190-572X</identifier><identifier>EISSN: 2190-5738</identifier><identifier>DOI: 10.1007/s13205-020-02441-9</identifier><identifier>PMID: 33088657</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Agriculture ; Anaerobic conditions ; Antiinfectives and antibacterials ; Bioinformatics ; Biological activity ; Biomaterials ; Biotechnology ; Cancer Research ; Chemistry ; Chemistry and Materials Science ; Homeostasis ; Membrane proteins ; Molecular dynamics ; Original ; Original Article ; Petroleum ether ; Plant extracts ; Protein structure ; Protein transport ; Proteins ; Salmonella ; Stem Cells ; Thin layer chromatography ; Topology ; Virulence</subject><ispartof>3 Biotech, 2020-10, Vol.10 (10), p.460-460, Article 460</ispartof><rights>King Abdulaziz City for Science and Technology 2020</rights><rights>King Abdulaziz City for Science and Technology 2020.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3899-9aaec7d74b533b0535a5b4b9f0c4619c63ccc98312e8b9764ede435508f5da503</citedby><cites>FETCH-LOGICAL-c3899-9aaec7d74b533b0535a5b4b9f0c4619c63ccc98312e8b9764ede435508f5da503</cites><orcidid>0000-0002-5529-075X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7527380/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7527380/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,41488,42557,51319,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33088657$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Veni, A.</creatorcontrib><creatorcontrib>Lokeswari, T. S.</creatorcontrib><creatorcontrib>Krishna Kumari, G. N.</creatorcontrib><creatorcontrib>Gayathri, D.</creatorcontrib><creatorcontrib>Sudandiradoss, C.</creatorcontrib><title>Bioactivity of melianone against Salmonella and in silico prediction of a membrane protein target</title><title>3 Biotech</title><addtitle>3 Biotech</addtitle><addtitle>3 Biotech</addtitle><description>Melianone, the protolimonoid (24, 25-epoxyflindissone), was isolated from the medicinal tree species,
Swietenia mahagoni
(L.) JACQ (Meliaceae). The compound isolated from petroleum ether leaf extracts (5.39%) was quantified using high-performance thin-layer chromatography (HPTLC) method. In antimicrobial assays melianone inhibited
Salmonella
ser
.
Typhi with an MIC of 0.053 µM. Induced Fit Docking (IFD) of the ligand, melianone, with proteins involved in anaerobic virulence of the pathogen, revealed that it binds with FocA (a transport protein of formate ions) at its “periplasmic opening” with a glide energy of − 51.8576 kcal mol
−1
. Melianone altered the overall conformation of the protein (protomer A) by 0.347 Å RMSD. It induced a notable protein topology (Ω loop region) shift in the channel from an intermediate-open to a closed-state conformation and was supported by molecular dynamic simulations performed. FocA, a protein that contributes to its survival under anaerobic conditions, was further evaluated experimentally, after exposure of
Salmonella
ser. Typhi to melianone, resulting in the altered homeostasis of formate.</description><subject>Agriculture</subject><subject>Anaerobic conditions</subject><subject>Antiinfectives and antibacterials</subject><subject>Bioinformatics</subject><subject>Biological activity</subject><subject>Biomaterials</subject><subject>Biotechnology</subject><subject>Cancer Research</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Homeostasis</subject><subject>Membrane proteins</subject><subject>Molecular dynamics</subject><subject>Original</subject><subject>Original Article</subject><subject>Petroleum ether</subject><subject>Plant extracts</subject><subject>Protein structure</subject><subject>Protein transport</subject><subject>Proteins</subject><subject>Salmonella</subject><subject>Stem Cells</subject><subject>Thin layer chromatography</subject><subject>Topology</subject><subject>Virulence</subject><issn>2190-572X</issn><issn>2190-5738</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp9kUtLxDAUhYMoOuj8ARdScOOmmkfTNhtBB18w4EIFd-E2TcdIm4xJZ8B_b-qM42NhICThfuckNwehQ4JPCcbFWSCMYp5iiuPMMpKKLTSiROCUF6zc3uzp8x4ah_CK4-CEC4J30R5juCxzXowQXBoHqjdL078nrkk63RqwzuoEZmBs6JMHaLt4bltIwNaJsUkwrVEumXtdmyh1dhBClHaVh6ice9fryPXgZ7o_QDsNtEGP1-s-erq-epzcptP7m7vJxTRVrBQiFQBaFXWRVZyxCnPGgVdZJRqsspwIlTOllCgZobqsRJFnutYZ4xyXDa-BY7aPzle-80XV6Vpp23to5dybDvy7dGDk74o1L3LmlrLgNP7YYHCyNvDubaFDLzsT1NC41W4RJM04y8siFwN6_Ad9dQtvY3sDhSknhA0UXVHKuxC8bjaPIVgOIcpViDKGKD9DlCKKjn62sZF8RRYBtgJCLNmZ9t93_2P7AadQqGE</recordid><startdate>20201001</startdate><enddate>20201001</enddate><creator>Veni, A.</creator><creator>Lokeswari, T. S.</creator><creator>Krishna Kumari, G. N.</creator><creator>Gayathri, D.</creator><creator>Sudandiradoss, C.</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-5529-075X</orcidid></search><sort><creationdate>20201001</creationdate><title>Bioactivity of melianone against Salmonella and in silico prediction of a membrane protein target</title><author>Veni, A. ; Lokeswari, T. S. ; Krishna Kumari, G. N. ; Gayathri, D. ; Sudandiradoss, C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3899-9aaec7d74b533b0535a5b4b9f0c4619c63ccc98312e8b9764ede435508f5da503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Agriculture</topic><topic>Anaerobic conditions</topic><topic>Antiinfectives and antibacterials</topic><topic>Bioinformatics</topic><topic>Biological activity</topic><topic>Biomaterials</topic><topic>Biotechnology</topic><topic>Cancer Research</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Homeostasis</topic><topic>Membrane proteins</topic><topic>Molecular dynamics</topic><topic>Original</topic><topic>Original Article</topic><topic>Petroleum ether</topic><topic>Plant extracts</topic><topic>Protein structure</topic><topic>Protein transport</topic><topic>Proteins</topic><topic>Salmonella</topic><topic>Stem Cells</topic><topic>Thin layer chromatography</topic><topic>Topology</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Veni, A.</creatorcontrib><creatorcontrib>Lokeswari, T. S.</creatorcontrib><creatorcontrib>Krishna Kumari, G. N.</creatorcontrib><creatorcontrib>Gayathri, D.</creatorcontrib><creatorcontrib>Sudandiradoss, C.</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>3 Biotech</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Veni, A.</au><au>Lokeswari, T. S.</au><au>Krishna Kumari, G. N.</au><au>Gayathri, D.</au><au>Sudandiradoss, C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bioactivity of melianone against Salmonella and in silico prediction of a membrane protein target</atitle><jtitle>3 Biotech</jtitle><stitle>3 Biotech</stitle><addtitle>3 Biotech</addtitle><date>2020-10-01</date><risdate>2020</risdate><volume>10</volume><issue>10</issue><spage>460</spage><epage>460</epage><pages>460-460</pages><artnum>460</artnum><issn>2190-572X</issn><eissn>2190-5738</eissn><abstract>Melianone, the protolimonoid (24, 25-epoxyflindissone), was isolated from the medicinal tree species,
Swietenia mahagoni
(L.) JACQ (Meliaceae). The compound isolated from petroleum ether leaf extracts (5.39%) was quantified using high-performance thin-layer chromatography (HPTLC) method. In antimicrobial assays melianone inhibited
Salmonella
ser
.
Typhi with an MIC of 0.053 µM. Induced Fit Docking (IFD) of the ligand, melianone, with proteins involved in anaerobic virulence of the pathogen, revealed that it binds with FocA (a transport protein of formate ions) at its “periplasmic opening” with a glide energy of − 51.8576 kcal mol
−1
. Melianone altered the overall conformation of the protein (protomer A) by 0.347 Å RMSD. It induced a notable protein topology (Ω loop region) shift in the channel from an intermediate-open to a closed-state conformation and was supported by molecular dynamic simulations performed. FocA, a protein that contributes to its survival under anaerobic conditions, was further evaluated experimentally, after exposure of
Salmonella
ser. Typhi to melianone, resulting in the altered homeostasis of formate.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>33088657</pmid><doi>10.1007/s13205-020-02441-9</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-5529-075X</orcidid><oa>free_for_read</oa></addata></record> |
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| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; SpringerNature Journals; PubMed Central |
| subjects | Agriculture Anaerobic conditions Antiinfectives and antibacterials Bioinformatics Biological activity Biomaterials Biotechnology Cancer Research Chemistry Chemistry and Materials Science Homeostasis Membrane proteins Molecular dynamics Original Original Article Petroleum ether Plant extracts Protein structure Protein transport Proteins Salmonella Stem Cells Thin layer chromatography Topology Virulence |
| title | Bioactivity of melianone against Salmonella and in silico prediction of a membrane protein target |
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