Structural Revision of Lydiamycin A by Reinvestigation of the Stereochemistry

Hwang, Sunghoon; Shin, Daniel; Kim, Tae Ho; An, Joon Soo; Jo, Shin-Il; Jang, Jichan; Hong, Suckchang; Shin, Jongheon; Oh, Dong‐Chan

doi:10.1021/acs.orglett.0c01110

Cited by 12 publications

(18 citation statements)

References 14 publications

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“…The position of C-2 was revised to S-configuration, instead of R as previously reported and C-19 and C-25 were assigned as S and R, respectively, which explained why none of four synthesized possible isomers based on the proposed structure with unassigned C-19 and C-25 displayed an NMR spectrum consistent with the natural compound. 18,20,21 Another route to piperazic acid employs Evans-type auxiliaries starting with bromide 18 (Fig. 6).…”

Section: Synthesis Of Free Piperazic Acidmentioning

confidence: 99%

Synthetic and biosynthetic routes to nitrogen–nitrogen bonds

Niikura

et al. 2022

Chem. Soc. Rev.

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Section: Synthesis Of Free Piperazic Acidmentioning

confidence: 99%

Synthetic and biosynthetic routes to nitrogen–nitrogen bonds

Niikura

et al. 2022

Chem. Soc. Rev.

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“…GG23 identified the production of lydiamycin A [15]. Detailed structure elucidation enabled us to revise the previously reported structure [16]. Analysis of the full genome of Streptomyces sp.…”

Section: Introductionmentioning

confidence: 97%

Pentaminomycins C–E: Cyclic Pentapeptides as Autophagy Inducers from a Mealworm Beetle Gut Bacterium

Hwang

Jo³

et al. 2020

Microorganisms

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Pentaminomycins C–E (1–3) were isolated from the culture of the Streptomyces sp. GG23 strain from the guts of the mealworm beetle, Tenebrio molitor. The structures of the pentaminomycins were determined to be cyclic pentapeptides containing a modified amino acid, N5-hydroxyarginine, based on 1D and 2D NMR and mass spectroscopic analyses. The absolute configurations of the amino acid residues were assigned using Marfey’s method and bioinformatics analysis of their nonribosomal peptide biosynthetic gene cluster (BGC). Detailed analysis of the BGC enabled us to propose that the structural variations in 1–3 originate from the low specificity of the adenylation domain in the nonribosomal peptide synthetase (NRPS) module 1, and indicate that macrocyclization can be catalyzed noncanonically by penicillin binding protein (PBP)-type TE. Furthermore, pentaminomycins C and D (1 and 2) showed significant autophagy-inducing activities and were cytoprotective against oxidative stress in vitro.

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“…One of the first bioactive molecules obtained from symbiotic actinomycetes in insect ecosystems is dentigerumycin, a piperazic acid-bearing antifungal cyclic peptide isolated from a Pseudonocardia symbiont found on the exoskeleton of a fungus-growing ant ( Apterostigma dentigerum ) . Subsequent chemical investigations of insect-associated actinomycetes have revealed that a Streptomyces strain found in the gut of a mealworm ( Tenebrio molitor ) produces lydiamycin A, an antitubercular cyclic peptide, and the pentaminomycin family of autophagy-inducing cyclic peptides. , Actinobacterial communities associated with carrion beetles have also produced multiple nonproteinogenic amino acid-bearing NRPs, such as antibacterial nicrophorusamides including 5-chloro-tryptophan and β-hydroxyasparagine from Microbacterium sp. found in the gut of Nicrophorus concolor and antitubercular coprisamides containing β-methylaspartic acid and 2,3-diaminopropanoic acid isolated from Micromonospora sp.…”

Section: Introductionmentioning

confidence: 99%

Azetidine-Bearing Non-Ribosomal Peptides, Bonnevillamides D and E, Isolated from a Carrion Beetle-Associated Actinomycete

et al. 2021

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Two new nonribosomal peptides, bonnevillamides D and E (1 and 2), have been discovered in Streptomyces sp. UTZ13 isolated from the carrion beetle, Nicrophorus concolor. Combinational analysis of the UV, MS, and NMR spectroscopic data revealed that their planar structures were comprised of dichlorinated linear peptides containing nonproteinogenic amino acid residues, such as 4methylazetidinecarboxylic acid and 4-O-acetyl-5-methylproline. The configurations of bonnevillamides D and E (1 and 2) were determined based on ROESY correlations, the advanced Marfey's method, phenylglycine methyl ester derivatization, molecular modeling, and circular dichroism spectroscopy. The nonribosomal peptide synthetase biosynthetic pathway of bonnevillamides D and E has been proposed using bioinformatic analysis of the whole-genome sequence data of Streptomyces sp. UTZ13. Their biological activity toward the aggregation of amyloid-β, which is one of the key pathogenic proteins in Alzheimer's disease, was evaluated using a thioflavin T assay and gel electrophoresis. Bonnevillamides D and E reversed the fibril formation by inducing the monomerization of amyloid-β aggregates.

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Structural Revision of Lydiamycin A by Reinvestigation of the Stereochemistry

Cited by 12 publications

References 14 publications

Synthetic and biosynthetic routes to nitrogen–nitrogen bonds

Synthetic and biosynthetic routes to nitrogen–nitrogen bonds

Pentaminomycins C–E: Cyclic Pentapeptides as Autophagy Inducers from a Mealworm Beetle Gut Bacterium

Azetidine-Bearing Non-Ribosomal Peptides, Bonnevillamides D and E, Isolated from a Carrion Beetle-Associated Actinomycete

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