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  1. Article ; Online: Methylation in hangtaimycin biosynthesis and its antibacterial activities.

    Luo, Minghe / Dong, Yulu / Deng, Zixin / Sun, Yuhui

    Synthetic and systems biotechnology

    2023  Volume 8, Issue 4, Page(s) 682–687

    Abstract: About two-thirds of small molecule drugs contain methyl group and it plays a very important role in the drug development. So, methyltransferases catalyzing the methylation have always attracted great attention. Hangtaimycin (HTM) is a potent ... ...

    Abstract About two-thirds of small molecule drugs contain methyl group and it plays a very important role in the drug development. So, methyltransferases catalyzing the methylation have always attracted great attention. Hangtaimycin (HTM) is a potent hepatoprotective agent. Previous study showed that its biosynthetic gene cluster contained three methyltransferase domains, but their characteristics in HTM biosynthetic pathway has not been revealed. In this study, we clarified multi-methylations in HTM biosynthesis in vivo. It showed that the two
    Language English
    Publishing date 2023-10-30
    Publishing country China
    Document type Journal Article
    ISSN 2405-805X
    ISSN (online) 2405-805X
    DOI 10.1016/j.synbio.2023.10.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Discovery of olimycin E from

    Tu, Lirong / Shen, Shumei / Yan, Zhenyang / Li, Xiaoxia / Liu, Kai / Xu, Jin / Luo, Minghe

    Natural product research

    2024  , Page(s) 1–6

    Abstract: A new natural product olimycin E ( ...

    Abstract A new natural product olimycin E (
    Language English
    Publishing date 2024-04-08
    Publishing country England
    Document type Journal Article
    ZDB-ID 2185747-7
    ISSN 1478-6427 ; 1478-6419
    ISSN (online) 1478-6427
    ISSN 1478-6419
    DOI 10.1080/14786419.2024.2337131
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  3. Article ; Online: Virtual screening and biological activity evaluation of novel efflux pump inhibitors targeting AdeB

    Tuo, Yan / Tang, Yuelu / Yang, Ran / Zhao, Xuemin / Luo, Minghe / Zhou, Xing / Wang, Yuanqiang

    International Journal of Biological Macromolecules. 2023 Aug. 04, p.126109-

    2023  , Page(s) 126109–

    Abstract: The AdeABC efflux pump is an important mechanism causing multidrug resistance in Acinetobacter baumannii, and its main component AdeB can recognize carbapenems, aminoglycosides, and other multi-class antibiotics and efflux them intracellularly, which is ... ...

    Abstract The AdeABC efflux pump is an important mechanism causing multidrug resistance in Acinetobacter baumannii, and its main component AdeB can recognize carbapenems, aminoglycosides, and other multi-class antibiotics and efflux them intracellularly, which is an ideal target for the development of anti-multidrug resistant bacteria drugs. Here, we combined multiple computer-aided drug design methods to target AdeB to identify promising novel structural inhibitors. Virtual screening was performed by molecular docking and molecular dynamics simulation (MD) and 12 potential compounds were identified from the databases. Meanwhile, their biological activities were validated by in vitro activity assays, and ChemDiv L676–2179 (γ-IFN), ChemDiv L676–1461, and Chembridge 53,717,615 were confirmed to suppress efflux effects and restore antibiotic susceptibility of resistant bacteria, which are expected to be developed as adjuvant drugs for the treatment of multi-drug resistant Acinetobacter baumannii clinical infections.
    Keywords Acinetobacter baumannii ; adjuvants ; aminoglycosides ; antibiotic resistance ; bioactive properties ; carbapenems ; drug design ; molecular dynamics ; multiple drug resistance ; transporters ; Multidrug-resistance Acinetobacter baumannii ; AdeABC efflux pump ; Virtual screening ; Molecular simulation ; Activity evaluation
    Language English
    Dates of publication 2023-0804
    Publishing place Elsevier B.V.
    Document type Article ; Online
    Note Pre-press version
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2023.126109
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  4. Article ; Online: BamA-targeted antimicrobial peptide design for enhanced efficacy and reduced toxicity.

    Yang, Li / Luo, Minghe / Liu, Zhou / Li, Yuepeng / Lin, Zhihua / Geng, Shan / Wang, Yuanqiang

    Amino acids

    2023  Volume 55, Issue 10, Page(s) 1317–1331

    Abstract: The emergence of drug-resistant superbugs has necessitated a pressing need for innovative antibiotics. Antimicrobial peptides (AMPs) have demonstrated broad-spectrum antibacterial activity, reduced susceptibility to resistance, and immunomodulatory ... ...

    Abstract The emergence of drug-resistant superbugs has necessitated a pressing need for innovative antibiotics. Antimicrobial peptides (AMPs) have demonstrated broad-spectrum antibacterial activity, reduced susceptibility to resistance, and immunomodulatory effects, rendering them promising for combating drug-resistant microorganisms. This study employed computational simulation methods to screen and design AMPs specifically targeting ESKAPE pathogens. Particularly, AMPs were rationally designed to target the BamA and obtain novel antimicrobial peptide sequences. The designed AMPs were assessed for their antibacterial activities, mechanisms, and stability. Molecular docking and dynamics simulations demonstrated the interaction of both designed AMPs, 11pep and D-11pep, with the β1, β9, β15, and β16 chains of BamA, resulting in misfolding of outer membrane proteins and antibacterial effects. Subsequent antibacterial investigations confirmed the broad-spectrum activity of both 11pep and D-11pep, with D-11pep demonstrating higher potency against resistant Gram-negative bacteria. D-11pep exhibited MICs of 16, 8, and 32 μg/mL against carbapenem-resistant Escherichia coli, carbapenem-resistant Pseudomonas aeruginosa, and multi-drug-resistant Acinetobacter baumannii, respectively, with a concomitant lower resistance induction. Mechanism of action studies confirmed that peptides could disrupt the bacterial outer membrane, aligning with the findings of molecular dynamics simulations. Additionally, D-11pep demonstrated superior stability and reduced toxicity in comparison to 11pep. The findings of this study underscore the efficacy of rational AMP design that targets BamA, along with the utilization of D-amino acid replacements as a strategy for developing AMPs against drug-resistant bacteria.
    MeSH term(s) Antimicrobial Peptides ; Antimicrobial Cationic Peptides/pharmacology ; Antimicrobial Cationic Peptides/chemistry ; Molecular Docking Simulation ; Anti-Bacterial Agents/chemistry ; Carbapenems ; Microbial Sensitivity Tests
    Chemical Substances Antimicrobial Peptides ; Antimicrobial Cationic Peptides ; Anti-Bacterial Agents ; Carbapenems
    Language English
    Publishing date 2023-09-05
    Publishing country Austria
    Document type Journal Article
    ZDB-ID 1121341-3
    ISSN 1438-2199 ; 0939-4451
    ISSN (online) 1438-2199
    ISSN 0939-4451
    DOI 10.1007/s00726-023-03307-z
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3490: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Virtual screening and biological activity evaluation of novel efflux pump inhibitors targeting AdeB.

    Tuo, Yan / Tang, Yuelu / Yang, Ran / Zhao, XueMin / Luo, Minghe / Zhou, Xing / Wang, Yuanqiang

    International journal of biological macromolecules

    2023  Volume 250, Page(s) 126109

    Abstract: The AdeABC efflux pump is an important mechanism causing multidrug resistance in Acinetobacter baumannii, and its main component AdeB can recognize carbapenems, aminoglycosides, and other multi-class antibiotics and efflux them intracellularly, which is ... ...

    Abstract The AdeABC efflux pump is an important mechanism causing multidrug resistance in Acinetobacter baumannii, and its main component AdeB can recognize carbapenems, aminoglycosides, and other multi-class antibiotics and efflux them intracellularly, which is an ideal target for the development of anti-multidrug resistant bacteria drugs. Here, we combined multiple computer-aided drug design methods to target AdeB to identify promising novel structural inhibitors. Virtual screening was performed by molecular docking and molecular dynamics simulation (MD) and 12 potential compounds were identified from the databases. Meanwhile, their biological activities were validated by in vitro activity assays, and ChemDiv L676-2179 (γ-IFN), ChemDiv L676-1461, and Chembridge 53717615 were confirmed to suppress efflux effects and restore antibiotic susceptibility of resistant bacteria, which are expected to be developed as adjuvant drugs for the treatment of multi-drug resistant Acinetobacter baumannii clinical infections.
    Language English
    Publishing date 2023-08-04
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2023.126109
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    In stock of ZB MED Cologne/Königswinter

    Zs.B 2374: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  6. Article: Two new streptovaricin derivatives from mutants of Streptomyces spectabilis CCTCC M2017417

    Luo, Minghe / Dong, Yulu / Tang, Lingjie / Chen, Xu / Hu, Zhiwei / Xie, Wenxinyu / Deng, Zixin / Sun, Yuhui

    Natural product research. 2022 July 15, v. 36, no. 14

    2022  

    Abstract: Two new ansamycin derivatives, damavaricin H (1) and protostreptovaricin VI (2) were isolated from the Streptomyces spectabilis CCTCC M2017417 derived mutants of ΔstvP5 and ΔstvA2, respectively. The structures of 1 and 2 were established by analysis of ... ...

    Abstract Two new ansamycin derivatives, damavaricin H (1) and protostreptovaricin VI (2) were isolated from the Streptomyces spectabilis CCTCC M2017417 derived mutants of ΔstvP5 and ΔstvA2, respectively. The structures of 1 and 2 were established by analysis of the HRESIMS as well as 1D and 2D NMR datasets. The minimum inhibitory concentration (MIC) results showed that compounds 1 and 2 possessed the corresponding anti-MRSA bioactivities of 4 ∼ 8 μg/ml and 8 ∼ 16 μg/ml, which confirmed the structure-activity relationships of streptovaricins reported previously and also revealed that addition of the hydroxyl group at C-8 increased the anti-MRSA activity.
    Keywords Streptomyces spectabilis ; data collection ; minimum inhibitory concentration ; research
    Language English
    Dates of publication 2022-0715
    Size p. 3689-3694.
    Publishing place Taylor & Francis
    Document type Article
    ZDB-ID 2185747-7
    ISSN 1478-6427 ; 1478-6419
    ISSN (online) 1478-6427
    ISSN 1478-6419
    DOI 10.1080/14786419.2021.1881517
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  7. Article: Antibacterial natural products lobophorin L and M from the marine-derived Streptomyces sp. 4506

    Luo, Minghe / Tang, Lingjie / Dong, Yulu / Huang, Hongbo / Deng, Zixin / Sun, Yuhui

    Natural product research. 2021 Dec. 17, v. 35, no. 24

    2021  

    Abstract: Two new spirotetronate natural products, lobophorin L (1) and lobophorin M (2), together with three known lobophorin-like spirotetronate antibiotics (3–5) and two known ansamycins (6–7), were isolated from the marine-derived Streptomyces sp. 4506. The ... ...

    Abstract Two new spirotetronate natural products, lobophorin L (1) and lobophorin M (2), together with three known lobophorin-like spirotetronate antibiotics (3–5) and two known ansamycins (6–7), were isolated from the marine-derived Streptomyces sp. 4506. The structures of 1 and 2 were established on the basis of HRESIMS as well as 1D and 2D NMR datasets. Antibacterial assay showed that, compounds 1 and 3–5 exhibited strong to moderate antibacterial activities against Micrococcus luteus and Bacillus thuringiensis with MIC values ranging from 0.0625 to 8 μg/mL, while compounds 3 and 6 showed weak antibacterial activities against Staphylococcus aureus and MRSA. The antibacterial activities of the lobophorins in this study indicated that the more substitution number of the sugar moieties at C-9 of the lobophorin, the stronger antimicrobial properties it may deserve, and the higher the oxidation degree of substituent group at C-3D, the better antibacterial activities of its corresponding compound could be.
    Keywords Bacillus thuringiensis ; Micrococcus luteus ; Streptomyces ; data collection ; methicillin-resistant Staphylococcus aureus ; oxidation ; research ; sugars
    Language English
    Dates of publication 2021-1217
    Size p. 5581-5587.
    Publishing place Taylor & Francis
    Document type Article
    ZDB-ID 2185747-7
    ISSN 1478-6427 ; 1478-6419
    ISSN (online) 1478-6427
    ISSN 1478-6419
    DOI 10.1080/14786419.2020.1797730
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  8. Article: Synthesis of tryptophan-dehydrobutyrine diketopiperazine and biological activity of hangtaimycin and its co-metabolites.

    Xu, Houchao / Wochele, Anne / Luo, Minghe / Schnakenburg, Gregor / Sun, Yuhui / Brötz-Oesterhelt, Heike / Dickschat, Jeroen S

    Beilstein journal of organic chemistry

    2022  Volume 18, Page(s) 1159–1165

    Abstract: An improved synthesis for tryptophan-dehydrobutyrine diketopiperazine (TDD), a co-metabolite of the hybrid polyketide/non-ribosomal peptide hangtaimycin, starting from ʟ-tryptophan is presented. Comparison to TDD isolated from the hangtaimycin ... ...

    Abstract An improved synthesis for tryptophan-dehydrobutyrine diketopiperazine (TDD), a co-metabolite of the hybrid polyketide/non-ribosomal peptide hangtaimycin, starting from ʟ-tryptophan is presented. Comparison to TDD isolated from the hangtaimycin producer
    Language English
    Publishing date 2022-09-07
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2192461-2
    ISSN 1860-5397
    ISSN 1860-5397
    DOI 10.3762/bjoc.18.120
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Subtly manipulating Zn

    Xiang, Jingjing / Luo, Minghe / Wu, Xingxing / Zhu, Yaofeng / Zhang, Xuan / Pan, Hongge / Sun, Wenping / Yan, Mi / Lu, Yingying / Jiang, Yinzhu

    Chemical communications (Cambridge, England)

    2022  Volume 58, Issue 65, Page(s) 9104–9107

    Abstract: By using ethylenediamine (En) as a complexing agent, the impact of various ... ...

    Abstract By using ethylenediamine (En) as a complexing agent, the impact of various Zn
    MeSH term(s) Electrodes ; Excipients ; Zinc
    Chemical Substances Excipients ; Zinc (J41CSQ7QDS)
    Language English
    Publishing date 2022-08-11
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d2cc02769k
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  10. Article: Subtly manipulating Zn²⁺-coordinated configurations with a complexing agent to boost the reversibility of the zinc anode

    Xiang, Jingjing / Luo, Minghe / Wu, Xingxing / Zhu, Yaofeng / Zhang, Xuan / Pan, Hongge / Sun, Wenping / Yan, Mi / Lu, Yingying / Jiang, Yinzhu

    Chemical communications. 2022 Aug. 11, v. 58, no. 65

    2022  

    Abstract: By using ethylenediamine (En) as a complexing agent, the impact of various Zn²⁺ coordinated configurations on Zn anode reversibility was systematically studied. With the predominant configurations of [Zn(En)]²⁺ and [Zn(En)₂]²⁺ in the electrolyte, both ... ...

    Abstract By using ethylenediamine (En) as a complexing agent, the impact of various Zn²⁺ coordinated configurations on Zn anode reversibility was systematically studied. With the predominant configurations of [Zn(En)]²⁺ and [Zn(En)₂]²⁺ in the electrolyte, both symmetric Zn/Zn cells and Zn/NiHCF full cells exhibit significantly improved cycling stability compared to the counterparts with pure ZnSO₄ electrolyte.
    Keywords anodes ; electrolytes ; ethylenediamines ; zinc
    Language English
    Dates of publication 2022-0811
    Size p. 9104-9107.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d2cc02769k
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