Margaret Brimble

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Distinguished Professor

University of Auckland

New Zealand

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About

Margaret Brimble is a Distinguished Professor at the University of Auckland, New Zealand. Her research areas encompass asymmetric total synthesis, natural product chemistry, and innovative approaches to enhancing bioavailability in pharmaceuticals. Recent articles highlight her work on the total synthesis of complex natural products and the development of novel synthetic methodologies for biologically active compounds.

Recent Grants

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Unleashing New Generation Lanthipeptides from Nature to Combat Antimicrobial Resistance

Open Date: 2019-01-01

Close Date: 2022-01-01

Grant: Close

Sweetening biological therapeutics-chemical synthesis of glycoprotein mimics

Open Date: 2019-01-01

Close Date: 2022-01-01

Grant: Close

Next-generation marine antifouling using designer peptides

Open Date: 2018-10-01

Close Date: 2021-09-30

Grant: Close

Westpac Trust Women of Influence Award (Science and Innovation)

Open Date: 2014-01-01

Close Date:

Grant: Close

MacDiarmid Medal

Open Date: 2012-01-01

Close Date:

Margaret Brimble

Research Interests

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About

Recent Grants

Articles (29)

Total Synthesis of (−)‐Cordycicadin D and 3,4‐trans‐Cordycicadins A and B: Entry to the 3,4‐trans‐Fused Cordycicadin Framework

Total Synthesis of (−)‐Cordycicadin D and 3,4‐trans‐Cordycicadins A and B: Entry to the 3,4‐trans‐Fused Cordycicadin Framework

Asymmetric Total Synthesis of (+)-Spiroapplanatumine G

Enhancing the Oral Bioavailability of Glutathione Using Innovative Analogue Approaches

Spiroketal natural products isolated from traditional Chinese medicine: isolation, biological activity, biosynthesis, and synthesis

Synthesis and α-Functionalisation of Cyclic Imines

Use of a Cyclic α-Alkylidene-β-Diketone as a Cleavable Linker Strategy for Antibody-Drug Conjugates

Late-Stage Desulfurization Enables Rapid and Efficient Solid-Phase Synthesis of Cathepsin-Cleavable Linkers for Antibody–Drug Conjugates

The Antimicrobial Peptide Capitellacin: Chemical Synthesis of Analogues to Probe the Role of Disulphide Bridges and Their Replacement with Vinyl Sulphides

The Enigma of Norbormide, a Rattus-Selective Toxicant

Synthesis, Structure–Activity Relationship Study, Bioactivity, and Nephrotoxicity Evaluation of the Proposed Structure of the Cyclic Lipodepsipeptide Brevicidine B

Creating New Antifoulants Using the Tools and Tactics of Medicinal Chemistry

Synthesis of the bicyclic butenolide core of pallamolide A: a biomimetic approach

A Stable Dehydratase Complex Catalyzes the Formation of Dehydrated Amino Acids in a Class V Lanthipeptide

Activity and cryo-EM structure of the polymerase domain of the human norovirus ProPol precursor

Synthesis of the Spirocyclic Imine Fragment of Portimines Using a γ-Hydroxymethyl-α,β-butenolide Dienophile in a Diastereoselective Diels–Alder Reaction

N-Substituted Iminothiolane (NIT): A Promising Strategy for Protecting Lysine Side Chains for Solid-Phase Peptide Chemistry

Antimicrobial Peptides Incorporating Halogenated Marine-Derived Amino Acid Substituents

On-Resin Conjugation of the Ruthenium Anticancer Agent Plecstatin-1 to Peptide Vectors

Azide–Enolate Cycloaddition‐Rearrangement Enables Direct α‐Amination of Amides and Enelactam Synthesis from Esters

Azide–Enolate Cycloaddition‐Rearrangement Enables Direct α‐Amination of Amides and Enelactam Synthesis from Esters**

Front Cover: Azide–Enolate Cycloaddition‐Rearrangement Enables Direct α‐Amination of Amides and Enelactam Synthesis from Esters (Chem. Eur. J. 31/2023)

Total Synthesis of Spiroketal Alkaloids Lycibarbarines A–C

NMR Shows Why a Small Chemical Change Almost Abolishes the Antimicrobial Activity of Glycocin F

Chemoselective Methods for Labeling and Modification of Peptides and Proteins

Nature-Inspired Peptide Antifouling Biocide: Coating Compatibility, Field Validation, and Environmental Stability

Flow-Based Fmoc-SPPS Preparation and SAR Study of Cathelicidin-PY Reveals Selective Antimicrobial Activity

The Leptospermum scoparium (Mānuka)-Specific Nectar and Honey Compound 3,6,7-Trimethyllumazine (LepteridineTM) That Inhibits Matrix Metalloproteinase 9 (MMP-9) Activity

Crystal Structure of Inhibitor-Bound GII.4 Sydney 2012 Norovirus 3C-Like Protease

Collaborators (14)

Patrick Cahill

Ghader Bashiri

Kerry M. Loomes

Fredrik Björkling

Alan J. Cameron

Kurt L. Krause

David Goldstone

Gillian E. Norris

Phillip Grant

Daniel Furkert

Christian Hartinger

Geoffrey Jameson

Vernon Ward

Paul. W. R. Harris

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