Karolina Wojtczak, Emilie Gillon, Diana Bura, Karen Richmond, Megan Joyce, Emma Caraher, Keela Kessie, Trinidad Velasco-Torrijos, Cristina Trujillo, Anne Imberty, Kevin Kavanagh, Gordon Cooke, Joseph P Byrne
{"title":"针对病原菌铜绿假单胞菌和白色念珠菌的抗粘附糖结合金属配合物。","authors":"Karolina Wojtczak, Emilie Gillon, Diana Bura, Karen Richmond, Megan Joyce, Emma Caraher, Keela Kessie, Trinidad Velasco-Torrijos, Cristina Trujillo, Anne Imberty, Kevin Kavanagh, Gordon Cooke, Joseph P Byrne","doi":"10.1039/d5ob00970g","DOIUrl":null,"url":null,"abstract":"<p><p>Glycoconjugates are known to interact with carbohydrate-binding proteins involved in adhesion by pathogens, and offer opportunities to design antimicrobial agents. Metal complexes with Eu(III), Ni(II) and Zn(II) were prepared from glycoconjugate ligand 1Gal, which binds to <i>P. aeruginosa</i>'s lectin LecA (<i>K</i><sub>d</sub> 9.6 ± 0.7 μM). <i>In vitro</i> anti-adhesive activity of these compounds was evaluated for both <i>P. aeruginosa</i> and <i>C. albicans</i>. Choice of metal ion played a crucial role in modulating anti-adhesive activity, with Eu(III) complexes most effective: [Eu·(1Gal)(H<sub>2</sub>O)<sub>6</sub>](CF<sub>3</sub>SO<sub>3</sub>)<sub>3</sub> inhibits 60% biofilm formation by <i>P. aeruginosa</i> and [Eu·(1Gal)<sub>3</sub>](CF<sub>3</sub>SO<sub>3</sub>)<sub>3</sub> inhibits 62% of <i>C. albicans</i> adhesion to buccal epithelial cells (both at 0.1 mM). The results presented demonstrate the potential for metal coordination to significantly enhance biological activity of glycoconjugates, surpassing the effect of the ligand's modest lectin-binding affinity alone.</p>","PeriodicalId":96,"journal":{"name":"Organic & Biomolecular Chemistry","volume":" ","pages":""},"PeriodicalIF":2.7000,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Antiadhesive glycoconjugate metal complexes targeting pathogens <i>Pseudomonas aeruginosa</i> and <i>Candida albicans</i>.\",\"authors\":\"Karolina Wojtczak, Emilie Gillon, Diana Bura, Karen Richmond, Megan Joyce, Emma Caraher, Keela Kessie, Trinidad Velasco-Torrijos, Cristina Trujillo, Anne Imberty, Kevin Kavanagh, Gordon Cooke, Joseph P Byrne\",\"doi\":\"10.1039/d5ob00970g\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Glycoconjugates are known to interact with carbohydrate-binding proteins involved in adhesion by pathogens, and offer opportunities to design antimicrobial agents. Metal complexes with Eu(III), Ni(II) and Zn(II) were prepared from glycoconjugate ligand 1Gal, which binds to <i>P. aeruginosa</i>'s lectin LecA (<i>K</i><sub>d</sub> 9.6 ± 0.7 μM). <i>In vitro</i> anti-adhesive activity of these compounds was evaluated for both <i>P. aeruginosa</i> and <i>C. albicans</i>. Choice of metal ion played a crucial role in modulating anti-adhesive activity, with Eu(III) complexes most effective: [Eu·(1Gal)(H<sub>2</sub>O)<sub>6</sub>](CF<sub>3</sub>SO<sub>3</sub>)<sub>3</sub> inhibits 60% biofilm formation by <i>P. aeruginosa</i> and [Eu·(1Gal)<sub>3</sub>](CF<sub>3</sub>SO<sub>3</sub>)<sub>3</sub> inhibits 62% of <i>C. albicans</i> adhesion to buccal epithelial cells (both at 0.1 mM). The results presented demonstrate the potential for metal coordination to significantly enhance biological activity of glycoconjugates, surpassing the effect of the ligand's modest lectin-binding affinity alone.</p>\",\"PeriodicalId\":96,\"journal\":{\"name\":\"Organic & Biomolecular Chemistry\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":2.7000,\"publicationDate\":\"2025-07-02\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Organic & Biomolecular Chemistry\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.1039/d5ob00970g\",\"RegionNum\":3,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, ORGANIC\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Organic & Biomolecular Chemistry","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1039/d5ob00970g","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, ORGANIC","Score":null,"Total":0}
Antiadhesive glycoconjugate metal complexes targeting pathogens Pseudomonas aeruginosa and Candida albicans.
Glycoconjugates are known to interact with carbohydrate-binding proteins involved in adhesion by pathogens, and offer opportunities to design antimicrobial agents. Metal complexes with Eu(III), Ni(II) and Zn(II) were prepared from glycoconjugate ligand 1Gal, which binds to P. aeruginosa's lectin LecA (Kd 9.6 ± 0.7 μM). In vitro anti-adhesive activity of these compounds was evaluated for both P. aeruginosa and C. albicans. Choice of metal ion played a crucial role in modulating anti-adhesive activity, with Eu(III) complexes most effective: [Eu·(1Gal)(H2O)6](CF3SO3)3 inhibits 60% biofilm formation by P. aeruginosa and [Eu·(1Gal)3](CF3SO3)3 inhibits 62% of C. albicans adhesion to buccal epithelial cells (both at 0.1 mM). The results presented demonstrate the potential for metal coordination to significantly enhance biological activity of glycoconjugates, surpassing the effect of the ligand's modest lectin-binding affinity alone.
期刊介绍：
Organic & Biomolecular Chemistry is an international journal using integrated research in chemistry-organic chemistry. Founded in 2003 by the Royal Society of Chemistry, the journal is published in Semimonthly issues and has been indexed by SCIE, a leading international database. The journal focuses on the key research and cutting-edge progress in the field of chemistry-organic chemistry, publishes and reports the research results in this field in a timely manner, and is committed to becoming a window and platform for rapid academic exchanges among peers in this field. The journal's impact factor in 2023 is 2.9, and its CiteScore is 5.5.
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