Lauren Murray

Total Synthesis Establishes the Biosynthetic Pathway to the Naphterpin and Marinone Natural Products

Publisher: Wiley

Date: 23-07-2018

DOI: 10.1002/ANIE.201804351

Biomimetic synthesis of the non-canonical PPAP natural products yezo'otogirin C and hypermogin D, and studies towards the synthesis of norascyronone A.

Publisher: Royal Society of Chemistry (RSC)

Date: 2022

DOI: 10.1039/D2OB00074A

Abstract: Oxidative degradation and rearrangement of polycyclic polyprenylated acylphloroglucinols (PPAPs) has created erse families of unique natural products that are attractive targets for biomimetic synthesis. Herein, we report a racemic synthesis of hyperibrin A and its oxidative radical cyclization to give yezo'otogirin C, followed by epoxidation and House-Meinwald rearrangement to give hypermogin D. We also investigated the biomimetic synthesis of norascyronone A

Structural Basis of Stereospecific Vanadium-Dependent Haloperoxidase Family Enzymes in Napyradiomycin Biosynthesis

Publisher: American Chemical Society (ACS)

Date: 19-08-2022

DOI: 10.1021/ACS.BIOCHEM.2C00338

Abstract: Vanadium-dependent haloperoxidases (VHPOs) from

Structure of the sliding clamp from the fungal pathogen Aspergillus fumigatus (AfumPCNA) and interactions with Human p21

Publisher: Wiley

Date: 27-02-2017

DOI: 10.1111/FEBS.14035

Abstract: The fungal pathogen Aspergillus fumigatus has been implicated in a drastic increase in life-threatening infections over the past decade. However, compared to other microbial pathogens, little is known about the essential molecular processes of this organism. One such fundamental process is DNA replication. The protein responsible for ensuring processive DNA replication is PCNA (proliferating cell nuclear antigen, also known as the sliding cl ), which cl s the replicative polymerase to DNA. Here we present the first crystal structure of a sliding cl from a pathogenic fungus (A. fumigatus), at 2.6Å. Surprisingly, the structure bears more similarity to the human sliding cl than other available fungal sliding cl s. Reflecting this, fluorescence polarization experiments demonstrated that AfumPCNA interacts with the PCNA-interacting protein (PIP-box) motif of human p21 with an affinity (K The atomic coordinates and structure factors for the Aspergillus fumigatus sliding cl can be found in the RCSB Protein Data Bank (www.rcsb.org) under the accession code 5TUP.

Total Enzyme Syntheses of Napyradiomycins A1 and B1

Publisher: American Chemical Society (ACS)

Date: 10-12-2018

DOI: 10.1021/JACS.8B10134

Biocatalytic oxidative cross-coupling reactions for biaryl bond formation

Publisher: Springer Science and Business Media LLC

Date: 02-03-2022

DOI: 10.1038/S41586-021-04365-7

Total Synthesis of Naphterpin and Marinone Natural Products

Publisher: American Chemical Society (ACS)

Date: 24-09-2019

DOI: 10.1021/ACS.ORGLETT.9B03095

Abstract: A concise and ergent strategy for the synthesis of the naphterpin and marinone meroterpenoid families has been developed. The approach features a succession of pericyclic reactions-an aromatic Claisen rearrangement, a retro-6π-electrocyclization, and two Diels-Alder reactions-which facilitated the first total synthesis of naphterpin itself in five steps from 2,5-dimethoxyphenol, alongside similar syntheses of 7-demethylnaphterpin and debromomarinone. Late-stage oxidation and bromination reactions were also investigated, leading to the first total syntheses of naphterpins B and C and isomarinone.

Meroterpenoid natural products fromStreptomycesbacteria – the evolution of chemoenzymatic syntheses

Publisher: Royal Society of Chemistry (RSC)

Date: 2020

DOI: 10.1039/D0NP00018C

Abstract: A review of the chemical ersity, biosynthesis, synthesis and biocatalysis of naphthoquinone-based meroterpenoids is presented.

A Diazo-Hooker Reaction, Inspired by the Biosynthesis of Azamerone

Publisher: American Chemical Society (ACS)

Date: 07-01-2022

DOI: 10.1021/ACS.ORGLETT.1C03810

Biaryl bond formation through biocatalytic oxidative cross-coupling reactions

Publisher: American Chemical Society (ACS)

Date: 04-08-2021

DOI: 10.26434/CHEMRXIV-2021-V0BV6

Abstract: Biocatalysis offers compelling advantages in synthesis, often becoming the method of choice based on sustainability, safety, and selectivity considerations. Despite these advantages, enzymes in synthesis are typically dedicated to functional group interconversions in linear synthetic sequences and have not been broadly integrated into the retrosynthetic logic for carbon skeleton assembly. In this article, we disclose a biocatalytic platform for fragment coupling to assemble target molecules convergently. Specifically, we report a strategy for biocatalytic phenolic cross-coupling through oxidative C–C bond formation. Using cytochrome P450 enzymes, we demonstrate the ability to catalyze cross-coupling reactions on a panel of phenolic substrates and further demonstrate the ability to tune these catalysts to possess the desired reactivity, site-, and atroposelectivity. This streamlined method for constructing sterically-hindered biaryl bonds provides an engineerable platform for assembling molecules with programmable catalyst-controlled reactivity and selectivity unprecedented with small molecule catalysts.

University Of Adelaide

Location: Australia

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University Of Michigan

Location: United States of America

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Discovery Early Career Researcher Award - Grant ID: DE240100502

Start Date: 2024

End Date: 12-2026

Amount: $424,875.00

Funder: Australian Research Council