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psim  (Twist Bioscience)

 
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    Twist Bioscience psim
    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
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    1) Product Images from "Complete biosynthesis of psychedelic tryptamines from three kingdoms in plants"

    Article Title: Complete biosynthesis of psychedelic tryptamines from three kingdoms in plants

    Journal: Science Advances

    doi: 10.1126/sciadv.aeb3034

    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , PsiM , and PsiK , or ( B ) OsCYP71P1 , RmNMT , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
    Figure Legend Snippet: Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , PsiM , and PsiK , or ( B ) OsCYP71P1 , RmNMT , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).

    Techniques Used: Comparison, Expressing, Mutagenesis, Two Tailed Test, Variant Assay, Residue



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    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
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    Journal: Science Advances

    Article Title: Complete biosynthesis of psychedelic tryptamines from three kingdoms in plants

    doi: 10.1126/sciadv.aeb3034

    Figure Lengend Snippet: Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , PsiM , and PsiK , or ( B ) OsCYP71P1 , RmNMT , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).

    Article Snippet: RmNMT , PsiH , PsiK , PsiM , OsCYP71P1 , AtCOMT , AtCOMTA160G , RebF , RebH , PyrH , and SttH coding sequences were codon optimized for expression in N. tabacum and synthesized by Twist Biosciences.

    Techniques: Comparison, Expressing, Mutagenesis, Two Tailed Test, Variant Assay, Residue

    Comparison of the technical details of the algorithms used in each of the three most cited articles presented in the clusters (1–6).

    Journal: Heliyon

    Article Title: Fault diagnosis of photovoltaic systems using artificial intelligence: A bibliometric approach

    doi: 10.1016/j.heliyon.2023.e21491

    Figure Lengend Snippet: Comparison of the technical details of the algorithms used in each of the three most cited articles presented in the clusters (1–6).

    Article Snippet: , , Detection and Classification , 100 , ✓ , ✓ , String disconnection and short-circuit , 740 , Matlab Simulink and PSIM , Probabilistic neural network , 1 min.

    Techniques: Comparison, Biomarker Discovery, Software, Sampling, Plasmid Preparation