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The potential target of bithionol against Staphylococcus aureus: design, synthesis and application of biotinylated probes Bio-A2
This study aims to explore the potential targets of bithionol in Staphylococcus aureus .The four bithionol biotinylated probes Bio-A2-1 , Bio-A2-2 , Bio-A2-3 , and Bio-A2-4 were synthesized, the minimal inhibitory concentrations (MICs) of these probes against S. aureus were determined. The bithionol...
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Published in: | Journal of antibiotics 2023-07, Vol.76 (7), p.406-415 |
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container_issue | 7 |
container_start_page | 406 |
container_title | Journal of antibiotics |
container_volume | 76 |
creator | Luo, Yue Wen, Zewen Xiong, Yanpeng Chen, Xuecheng Shen, Zonglin Li, Peiyu Peng, Yalan Deng, Qiwen Yu, Zhijian Zheng, Jinxin Han, Shiqing |
description | This study aims to explore the potential targets of bithionol in
Staphylococcus aureus
.The four bithionol biotinylated probes
Bio-A2-1
,
Bio-A2-2
,
Bio-A2-3
, and
Bio-A2-4
were synthesized, the minimal inhibitory concentrations (MICs) of these probes against
S. aureus
were determined. The bithionol binding proteins in
S. aureus
were identified through immunoprecipitation and LC-MS/MS with bithionol biotinylated probe. The biotinylated bithionol probes
Bio-A2-1
and
Bio-A2-3
displayed antibacterial activities against
S. aureus
. The
Bio-A2-1
showed lower MICs than
Bio-A2-3
, and both with the MIC
50
/MIC
90
at 12.5/12.5 μM against
S. aureus
clinical isolates. The inhibition rates of bithionol biotinylated probes
Bio-A2-1
and
Bio-A2-3
on the biofilm formation of
S. aureus
were comparable to that of bithionol, and were stronger than that of
Bio-A2-2
and
Bio-A2-4
. The biofilm formation of 10 out of 12
S. aureus
clinical isolates could be inhibited by
Bio-A2-1
(at 1/4×, or 1/2× MICs). There are three proteins identified in
S. aureus
through immunoprecipitation and LC-MS/MS with bithionol biotinylated probe
Bio-A2-1
: Protein translocase subunit SecA 1 (
secA1
), Alanine--tRNA ligase (
alaS
) and DNA gyrase subunit A (
gyrA
), and in which the SecA1 protein the highest coverage and the most unique peptides. The LYS112, GLN143, ASP213, GLY496 and ASP498 of SecA1 protein act as hydrogen acceptors to form 6 hydrogen bonds with bithionol biotinylated probe
Bio-A2-1
by molecular docking analysis. In conclusion, the bithionol biotinylated probe
Bio-A2-1
has antibacterial and anti-biofilm activities against
S. aureus
, and SecA1 was probably one of the potential targets of bithionol in
S. aureus
. |
doi_str_mv | 10.1038/s41429-023-00618-x |
format | article |
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Staphylococcus aureus
.The four bithionol biotinylated probes
Bio-A2-1
,
Bio-A2-2
,
Bio-A2-3
, and
Bio-A2-4
were synthesized, the minimal inhibitory concentrations (MICs) of these probes against
S. aureus
were determined. The bithionol binding proteins in
S. aureus
were identified through immunoprecipitation and LC-MS/MS with bithionol biotinylated probe. The biotinylated bithionol probes
Bio-A2-1
and
Bio-A2-3
displayed antibacterial activities against
S. aureus
. The
Bio-A2-1
showed lower MICs than
Bio-A2-3
, and both with the MIC
50
/MIC
90
at 12.5/12.5 μM against
S. aureus
clinical isolates. The inhibition rates of bithionol biotinylated probes
Bio-A2-1
and
Bio-A2-3
on the biofilm formation of
S. aureus
were comparable to that of bithionol, and were stronger than that of
Bio-A2-2
and
Bio-A2-4
. The biofilm formation of 10 out of 12
S. aureus
clinical isolates could be inhibited by
Bio-A2-1
(at 1/4×, or 1/2× MICs). There are three proteins identified in
S. aureus
through immunoprecipitation and LC-MS/MS with bithionol biotinylated probe
Bio-A2-1
: Protein translocase subunit SecA 1 (
secA1
), Alanine--tRNA ligase (
alaS
) and DNA gyrase subunit A (
gyrA
), and in which the SecA1 protein the highest coverage and the most unique peptides. The LYS112, GLN143, ASP213, GLY496 and ASP498 of SecA1 protein act as hydrogen acceptors to form 6 hydrogen bonds with bithionol biotinylated probe
Bio-A2-1
by molecular docking analysis. In conclusion, the bithionol biotinylated probe
Bio-A2-1
has antibacterial and anti-biofilm activities against
S. aureus
, and SecA1 was probably one of the potential targets of bithionol in
S. aureus
.</description><identifier>ISSN: 0021-8820</identifier><identifier>EISSN: 1881-1469</identifier><identifier>DOI: 10.1038/s41429-023-00618-x</identifier><identifier>PMID: 37185582</identifier><language>eng</language><publisher>Tokyo: Springer Japan</publisher><subject>631/326/22/1290 ; 631/92/609 ; 692/699/255/1318 ; 82 ; 82/58 ; Alanine ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - pharmacology ; Antibacterial activity ; Bacteriology ; Biofilms ; Biomedical and Life Sciences ; Bioorganic Chemistry ; Bithionol ; Chromatography, Liquid ; Clinical isolates ; DNA probes ; DNA topoisomerase ; Humans ; Hydrogen bonding ; Hydrogen bonds ; Immunoprecipitation ; Life Sciences ; Medicinal Chemistry ; Methicillin-Resistant Staphylococcus aureus ; Microbial Sensitivity Tests ; Microbiology ; Molecular docking ; Molecular Docking Simulation ; Organic Chemistry ; Peptides ; Probes ; Proteins ; Staphylococcal Infections - microbiology ; Staphylococcus aureus ; Staphylococcus aureus - genetics ; Tandem Mass Spectrometry ; Translocase ; tRNA Ala</subject><ispartof>Journal of antibiotics, 2023-07, Vol.76 (7), p.406-415</ispartof><rights>The Author(s), under exclusive licence to the Japan Antibiotics Research Association 2023. Springer Nature or its licensor (e.g. a society or other partner) 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><rights>2023. The Author(s), under exclusive licence to the Japan Antibiotics Research Association.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c399t-f38397b9bac4fcda21a2364a89fa17ceb69bf5d9fa8fc90db00150a6cfe430333</citedby><cites>FETCH-LOGICAL-c399t-f38397b9bac4fcda21a2364a89fa17ceb69bf5d9fa8fc90db00150a6cfe430333</cites><orcidid>0000-0003-4064-2430</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37185582$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Luo, Yue</creatorcontrib><creatorcontrib>Wen, Zewen</creatorcontrib><creatorcontrib>Xiong, Yanpeng</creatorcontrib><creatorcontrib>Chen, Xuecheng</creatorcontrib><creatorcontrib>Shen, Zonglin</creatorcontrib><creatorcontrib>Li, Peiyu</creatorcontrib><creatorcontrib>Peng, Yalan</creatorcontrib><creatorcontrib>Deng, Qiwen</creatorcontrib><creatorcontrib>Yu, Zhijian</creatorcontrib><creatorcontrib>Zheng, Jinxin</creatorcontrib><creatorcontrib>Han, Shiqing</creatorcontrib><title>The potential target of bithionol against Staphylococcus aureus: design, synthesis and application of biotinylated probes Bio-A2</title><title>Journal of antibiotics</title><addtitle>J Antibiot</addtitle><addtitle>J Antibiot (Tokyo)</addtitle><description>This study aims to explore the potential targets of bithionol in
Staphylococcus aureus
.The four bithionol biotinylated probes
Bio-A2-1
,
Bio-A2-2
,
Bio-A2-3
, and
Bio-A2-4
were synthesized, the minimal inhibitory concentrations (MICs) of these probes against
S. aureus
were determined. The bithionol binding proteins in
S. aureus
were identified through immunoprecipitation and LC-MS/MS with bithionol biotinylated probe. The biotinylated bithionol probes
Bio-A2-1
and
Bio-A2-3
displayed antibacterial activities against
S. aureus
. The
Bio-A2-1
showed lower MICs than
Bio-A2-3
, and both with the MIC
50
/MIC
90
at 12.5/12.5 μM against
S. aureus
clinical isolates. The inhibition rates of bithionol biotinylated probes
Bio-A2-1
and
Bio-A2-3
on the biofilm formation of
S. aureus
were comparable to that of bithionol, and were stronger than that of
Bio-A2-2
and
Bio-A2-4
. The biofilm formation of 10 out of 12
S. aureus
clinical isolates could be inhibited by
Bio-A2-1
(at 1/4×, or 1/2× MICs). There are three proteins identified in
S. aureus
through immunoprecipitation and LC-MS/MS with bithionol biotinylated probe
Bio-A2-1
: Protein translocase subunit SecA 1 (
secA1
), Alanine--tRNA ligase (
alaS
) and DNA gyrase subunit A (
gyrA
), and in which the SecA1 protein the highest coverage and the most unique peptides. The LYS112, GLN143, ASP213, GLY496 and ASP498 of SecA1 protein act as hydrogen acceptors to form 6 hydrogen bonds with bithionol biotinylated probe
Bio-A2-1
by molecular docking analysis. In conclusion, the bithionol biotinylated probe
Bio-A2-1
has antibacterial and anti-biofilm activities against
S. aureus
, and SecA1 was probably one of the potential targets of bithionol in
S. aureus
.</description><subject>631/326/22/1290</subject><subject>631/92/609</subject><subject>692/699/255/1318</subject><subject>82</subject><subject>82/58</subject><subject>Alanine</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antibacterial activity</subject><subject>Bacteriology</subject><subject>Biofilms</subject><subject>Biomedical and Life Sciences</subject><subject>Bioorganic Chemistry</subject><subject>Bithionol</subject><subject>Chromatography, Liquid</subject><subject>Clinical isolates</subject><subject>DNA probes</subject><subject>DNA topoisomerase</subject><subject>Humans</subject><subject>Hydrogen bonding</subject><subject>Hydrogen bonds</subject><subject>Immunoprecipitation</subject><subject>Life Sciences</subject><subject>Medicinal Chemistry</subject><subject>Methicillin-Resistant Staphylococcus aureus</subject><subject>Microbial Sensitivity Tests</subject><subject>Microbiology</subject><subject>Molecular docking</subject><subject>Molecular Docking Simulation</subject><subject>Organic Chemistry</subject><subject>Peptides</subject><subject>Probes</subject><subject>Proteins</subject><subject>Staphylococcal Infections - microbiology</subject><subject>Staphylococcus aureus</subject><subject>Staphylococcus aureus - genetics</subject><subject>Tandem Mass Spectrometry</subject><subject>Translocase</subject><subject>tRNA Ala</subject><issn>0021-8820</issn><issn>1881-1469</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNp9kU2LFDEQhoMo7rj6BzxIwIsHo_nq7sTbuvgFCx5cz6E6ncxk6UnaJA07N3-60V4VPHiqFPXUW4EHoaeMvmJUqNdFMsk1oVwQSnumyO09tGNKMcJkr--jHaWcEaU4PUOPSrmhVAxiUA_RmRiY6jrFd-j79cHhJVUXa4AZV8h7V3HyeAz1EFJMM4Y9hFgq_lJhOZzmZJO1a8GwZreWN3hyJezjS1xOsR7au03ihGFZ5mChtogtLdUQTzNUN-Elp9EV_DYkcsEfowce5uKe3NVz9PX9u-vLj-Tq84dPlxdXxAqtK_FCCT2MegQrvZ2AM-Cil6C0BzZYN_Z69N3UOuWtptNIKeso9NY7KagQ4hy92HLb9W-rK9UcQ7FuniG6tBbDFZMdl0Lqhj7_B71Ja47td43iumdSy75RfKNsTqVk582SwxHyyTBqfvoxmx_T_JhffsxtW3p2F72ORzf9WfktpAFiA0obxb3Lf2__J_YH_yueNQ</recordid><startdate>20230701</startdate><enddate>20230701</enddate><creator>Luo, Yue</creator><creator>Wen, Zewen</creator><creator>Xiong, Yanpeng</creator><creator>Chen, Xuecheng</creator><creator>Shen, Zonglin</creator><creator>Li, Peiyu</creator><creator>Peng, Yalan</creator><creator>Deng, Qiwen</creator><creator>Yu, Zhijian</creator><creator>Zheng, Jinxin</creator><creator>Han, Shiqing</creator><general>Springer Japan</general><general>Nature Publishing Group</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>3V.</scope><scope>7QL</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</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>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-4064-2430</orcidid></search><sort><creationdate>20230701</creationdate><title>The potential target of bithionol against Staphylococcus aureus: design, synthesis and application of biotinylated probes Bio-A2</title><author>Luo, Yue ; Wen, Zewen ; Xiong, Yanpeng ; Chen, Xuecheng ; Shen, Zonglin ; Li, Peiyu ; Peng, Yalan ; Deng, Qiwen ; Yu, Zhijian ; Zheng, Jinxin ; Han, Shiqing</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-f38397b9bac4fcda21a2364a89fa17ceb69bf5d9fa8fc90db00150a6cfe430333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>631/326/22/1290</topic><topic>631/92/609</topic><topic>692/699/255/1318</topic><topic>82</topic><topic>82/58</topic><topic>Alanine</topic><topic>Anti-Bacterial Agents - chemistry</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Antibacterial activity</topic><topic>Bacteriology</topic><topic>Biofilms</topic><topic>Biomedical and Life Sciences</topic><topic>Bioorganic Chemistry</topic><topic>Bithionol</topic><topic>Chromatography, Liquid</topic><topic>Clinical isolates</topic><topic>DNA probes</topic><topic>DNA topoisomerase</topic><topic>Humans</topic><topic>Hydrogen bonding</topic><topic>Hydrogen bonds</topic><topic>Immunoprecipitation</topic><topic>Life Sciences</topic><topic>Medicinal Chemistry</topic><topic>Methicillin-Resistant Staphylococcus aureus</topic><topic>Microbial Sensitivity Tests</topic><topic>Microbiology</topic><topic>Molecular docking</topic><topic>Molecular Docking Simulation</topic><topic>Organic Chemistry</topic><topic>Peptides</topic><topic>Probes</topic><topic>Proteins</topic><topic>Staphylococcal Infections - microbiology</topic><topic>Staphylococcus aureus</topic><topic>Staphylococcus aureus - genetics</topic><topic>Tandem Mass Spectrometry</topic><topic>Translocase</topic><topic>tRNA Ala</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Luo, Yue</creatorcontrib><creatorcontrib>Wen, Zewen</creatorcontrib><creatorcontrib>Xiong, Yanpeng</creatorcontrib><creatorcontrib>Chen, Xuecheng</creatorcontrib><creatorcontrib>Shen, Zonglin</creatorcontrib><creatorcontrib>Li, Peiyu</creatorcontrib><creatorcontrib>Peng, Yalan</creatorcontrib><creatorcontrib>Deng, Qiwen</creatorcontrib><creatorcontrib>Yu, Zhijian</creatorcontrib><creatorcontrib>Zheng, Jinxin</creatorcontrib><creatorcontrib>Han, Shiqing</creatorcontrib><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>ProQuest Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</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 One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Science Journals</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>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of antibiotics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Luo, Yue</au><au>Wen, Zewen</au><au>Xiong, Yanpeng</au><au>Chen, Xuecheng</au><au>Shen, Zonglin</au><au>Li, Peiyu</au><au>Peng, Yalan</au><au>Deng, Qiwen</au><au>Yu, Zhijian</au><au>Zheng, Jinxin</au><au>Han, Shiqing</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The potential target of bithionol against Staphylococcus aureus: design, synthesis and application of biotinylated probes Bio-A2</atitle><jtitle>Journal of antibiotics</jtitle><stitle>J Antibiot</stitle><addtitle>J Antibiot (Tokyo)</addtitle><date>2023-07-01</date><risdate>2023</risdate><volume>76</volume><issue>7</issue><spage>406</spage><epage>415</epage><pages>406-415</pages><issn>0021-8820</issn><eissn>1881-1469</eissn><abstract>This study aims to explore the potential targets of bithionol in
Staphylococcus aureus
.The four bithionol biotinylated probes
Bio-A2-1
,
Bio-A2-2
,
Bio-A2-3
, and
Bio-A2-4
were synthesized, the minimal inhibitory concentrations (MICs) of these probes against
S. aureus
were determined. The bithionol binding proteins in
S. aureus
were identified through immunoprecipitation and LC-MS/MS with bithionol biotinylated probe. The biotinylated bithionol probes
Bio-A2-1
and
Bio-A2-3
displayed antibacterial activities against
S. aureus
. The
Bio-A2-1
showed lower MICs than
Bio-A2-3
, and both with the MIC
50
/MIC
90
at 12.5/12.5 μM against
S. aureus
clinical isolates. The inhibition rates of bithionol biotinylated probes
Bio-A2-1
and
Bio-A2-3
on the biofilm formation of
S. aureus
were comparable to that of bithionol, and were stronger than that of
Bio-A2-2
and
Bio-A2-4
. The biofilm formation of 10 out of 12
S. aureus
clinical isolates could be inhibited by
Bio-A2-1
(at 1/4×, or 1/2× MICs). There are three proteins identified in
S. aureus
through immunoprecipitation and LC-MS/MS with bithionol biotinylated probe
Bio-A2-1
: Protein translocase subunit SecA 1 (
secA1
), Alanine--tRNA ligase (
alaS
) and DNA gyrase subunit A (
gyrA
), and in which the SecA1 protein the highest coverage and the most unique peptides. The LYS112, GLN143, ASP213, GLY496 and ASP498 of SecA1 protein act as hydrogen acceptors to form 6 hydrogen bonds with bithionol biotinylated probe
Bio-A2-1
by molecular docking analysis. In conclusion, the bithionol biotinylated probe
Bio-A2-1
has antibacterial and anti-biofilm activities against
S. aureus
, and SecA1 was probably one of the potential targets of bithionol in
S. aureus
.</abstract><cop>Tokyo</cop><pub>Springer Japan</pub><pmid>37185582</pmid><doi>10.1038/s41429-023-00618-x</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-4064-2430</orcidid></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0021-8820 |
ispartof | Journal of antibiotics, 2023-07, Vol.76 (7), p.406-415 |
issn | 0021-8820 1881-1469 |
language | eng |
recordid | cdi_proquest_miscellaneous_2814524349 |
source | Springer Link |
subjects | 631/326/22/1290 631/92/609 692/699/255/1318 82 82/58 Alanine Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology Antibacterial activity Bacteriology Biofilms Biomedical and Life Sciences Bioorganic Chemistry Bithionol Chromatography, Liquid Clinical isolates DNA probes DNA topoisomerase Humans Hydrogen bonding Hydrogen bonds Immunoprecipitation Life Sciences Medicinal Chemistry Methicillin-Resistant Staphylococcus aureus Microbial Sensitivity Tests Microbiology Molecular docking Molecular Docking Simulation Organic Chemistry Peptides Probes Proteins Staphylococcal Infections - microbiology Staphylococcus aureus Staphylococcus aureus - genetics Tandem Mass Spectrometry Translocase tRNA Ala |
title | The potential target of bithionol against Staphylococcus aureus: design, synthesis and application of biotinylated probes Bio-A2 |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T20%3A27%3A28IST&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=The%20potential%20target%20of%20bithionol%20against%20Staphylococcus%20aureus:%20design,%20synthesis%20and%20application%20of%20biotinylated%20probes%20Bio-A2&rft.jtitle=Journal%20of%20antibiotics&rft.au=Luo,%20Yue&rft.date=2023-07-01&rft.volume=76&rft.issue=7&rft.spage=406&rft.epage=415&rft.pages=406-415&rft.issn=0021-8820&rft.eissn=1881-1469&rft_id=info:doi/10.1038/s41429-023-00618-x&rft_dat=%3Cproquest_cross%3E2814524349%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c399t-f38397b9bac4fcda21a2364a89fa17ceb69bf5d9fa8fc90db00150a6cfe430333%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2829614946&rft_id=info:pmid/37185582&rfr_iscdi=true |