{"title":"针对甾醇14α-去甲基化酶和甾醇C-24甲基转移酶这两个利什曼原虫的关键蛋白,作为引人注目的治疗靶点的综合综述。","authors":"Diksha Kumari, Somdutt Mujwar, Kuljit Singh","doi":"10.1016/j.bioorg.2025.109046","DOIUrl":null,"url":null,"abstract":"<p><p>Leishmaniasis, a neglected tropical disease, poses a significant global health challenge mainly in tropical and subtropical areas. The limited treatment alternatives, coupled with significant associated toxicity, necessitate the requirement to identify new chemical scaffolds with reduced toxicity and improved efficacy. The two essential enzymes of the sterol biosynthetic pathway, Sterol C-24 methyl transferase (SMT) and Sterol 14α-demethylase (SDM), hold great promise as plausible drug targets due to their essentiality for parasite survival and virulence, along with exhibiting minimal homology with human counterparts. The present review discusses the importance of targeting leishmanial SDM and SMT proteins in the perquisite for anti-leishmanial drug discovery. We have performed a comprehensive search using various databases and created a small-molecule sterol inhibitor library, and by utilizing computational biology approaches, we tried to meticulously understand enzyme-inhibitor interactions of the library molecules with the leishmanial SMT and SDM proteins. Information pertaining to the chemical structure of the inhibitors, binding affinities, and interacting residues with both the proteins that drive their mode of action towards them has been elucidated. Thus, this review addresses inclusive information on Leishmanial SMT and SDM proteins, which can aid in unraveling new molecules to fight against the deadly parasitic infection by leveraging computational tools.</p>","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":"165 ","pages":"109046"},"PeriodicalIF":4.7000,"publicationDate":"2025-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"A comprehensive review of targeting sterol 14α-demethylase and sterol C-24 methyl transferase, two pivotal proteins in Leishmania, as compelling therapeutic targets.\",\"authors\":\"Diksha Kumari, Somdutt Mujwar, Kuljit Singh\",\"doi\":\"10.1016/j.bioorg.2025.109046\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Leishmaniasis, a neglected tropical disease, poses a significant global health challenge mainly in tropical and subtropical areas. The limited treatment alternatives, coupled with significant associated toxicity, necessitate the requirement to identify new chemical scaffolds with reduced toxicity and improved efficacy. The two essential enzymes of the sterol biosynthetic pathway, Sterol C-24 methyl transferase (SMT) and Sterol 14α-demethylase (SDM), hold great promise as plausible drug targets due to their essentiality for parasite survival and virulence, along with exhibiting minimal homology with human counterparts. The present review discusses the importance of targeting leishmanial SDM and SMT proteins in the perquisite for anti-leishmanial drug discovery. We have performed a comprehensive search using various databases and created a small-molecule sterol inhibitor library, and by utilizing computational biology approaches, we tried to meticulously understand enzyme-inhibitor interactions of the library molecules with the leishmanial SMT and SDM proteins. Information pertaining to the chemical structure of the inhibitors, binding affinities, and interacting residues with both the proteins that drive their mode of action towards them has been elucidated. Thus, this review addresses inclusive information on Leishmanial SMT and SDM proteins, which can aid in unraveling new molecules to fight against the deadly parasitic infection by leveraging computational tools.</p>\",\"PeriodicalId\":257,\"journal\":{\"name\":\"Bioorganic Chemistry\",\"volume\":\"165 \",\"pages\":\"109046\"},\"PeriodicalIF\":4.7000,\"publicationDate\":\"2025-09-27\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioorganic Chemistry\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.1016/j.bioorg.2025.109046\",\"RegionNum\":2,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioorganic Chemistry","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1016/j.bioorg.2025.109046","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
A comprehensive review of targeting sterol 14α-demethylase and sterol C-24 methyl transferase, two pivotal proteins in Leishmania, as compelling therapeutic targets.
Leishmaniasis, a neglected tropical disease, poses a significant global health challenge mainly in tropical and subtropical areas. The limited treatment alternatives, coupled with significant associated toxicity, necessitate the requirement to identify new chemical scaffolds with reduced toxicity and improved efficacy. The two essential enzymes of the sterol biosynthetic pathway, Sterol C-24 methyl transferase (SMT) and Sterol 14α-demethylase (SDM), hold great promise as plausible drug targets due to their essentiality for parasite survival and virulence, along with exhibiting minimal homology with human counterparts. The present review discusses the importance of targeting leishmanial SDM and SMT proteins in the perquisite for anti-leishmanial drug discovery. We have performed a comprehensive search using various databases and created a small-molecule sterol inhibitor library, and by utilizing computational biology approaches, we tried to meticulously understand enzyme-inhibitor interactions of the library molecules with the leishmanial SMT and SDM proteins. Information pertaining to the chemical structure of the inhibitors, binding affinities, and interacting residues with both the proteins that drive their mode of action towards them has been elucidated. Thus, this review addresses inclusive information on Leishmanial SMT and SDM proteins, which can aid in unraveling new molecules to fight against the deadly parasitic infection by leveraging computational tools.
期刊介绍:
Bioorganic Chemistry publishes research that addresses biological questions at the molecular level, using organic chemistry and principles of physical organic chemistry. The scope of the journal covers a range of topics at the organic chemistry-biology interface, including: enzyme catalysis, biotransformation and enzyme inhibition; nucleic acids chemistry; medicinal chemistry; natural product chemistry, natural product synthesis and natural product biosynthesis; antimicrobial agents; lipid and peptide chemistry; biophysical chemistry; biological probes; bio-orthogonal chemistry and biomimetic chemistry.
For manuscripts dealing with synthetic bioactive compounds, the Journal requires that the molecular target of the compounds described must be known, and must be demonstrated experimentally in the manuscript. For studies involving natural products, if the molecular target is unknown, some data beyond simple cell-based toxicity studies to provide insight into the mechanism of action is required. Studies supported by molecular docking are welcome, but must be supported by experimental data. The Journal does not consider manuscripts that are purely theoretical or computational in nature.
The Journal publishes regular articles, short communications and reviews. Reviews are normally invited by Editors or Editorial Board members. Authors of unsolicited reviews should first contact an Editor or Editorial Board member to determine whether the proposed article is within the scope of the Journal.