Discovery of Lithospermate B as a Potential Ligand for the Malarial E2 Ubiquitin-Conjugating Enzyme via Multiplexed Native Mass Spectrometry

There is an urgent need for novel therapeutics to combat <i>Plasmodium falciparum</i>, especially in light of increasing drug resistance. Here, we present a multiplexed native mass spectrometry (MS) platform capable of simultaneously screening multiple protein targets against chemically...

Full description

Saved in:
Bibliographic Details
Main Authors: Jianying Han, Wesley C. Van Voorhis, Ronald J. Quinn, Miaomiao Liu
Format: Article
Language:English
Published: MDPI AG 2025-05-01
Series:Chemosensors
Subjects:
Online Access:https://www.mdpi.com/2227-9040/13/5/166
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1849711748817354752
author Jianying Han
Wesley C. Van Voorhis
Ronald J. Quinn
Miaomiao Liu
author_facet Jianying Han
Wesley C. Van Voorhis
Ronald J. Quinn
Miaomiao Liu
author_sort Jianying Han
collection DOAJ
description There is an urgent need for novel therapeutics to combat <i>Plasmodium falciparum</i>, especially in light of increasing drug resistance. Here, we present a multiplexed native mass spectrometry (MS) platform capable of simultaneously screening multiple protein targets against chemically diverse crude extracts with minimal sample preparation. A mixture of seven malarial proteins was analyzed under optimized native MS conditions, enabling the detection of specific ligand binding events. Using this platform, lithospermate B from <i>Salvia miltiorrhiza</i> (Danshen) was identified as a novel ligand for a malarial ubiquitin-conjugating enzyme with moderate affinity (Kd = 30.5 ± 2.5 μM). This is the first report linking lithospermate B to a malarial protein target, highlighting the potential of native MS to uncover new bioactivities of known natural products. This approach significantly enhances the throughput of protein–ligand screening and offers a powerful tool for early-stage natural product-based drug discovery.
format Article
id doaj-art-fe79cce4897b4d489cec383d275ff1d9
institution DOAJ
issn 2227-9040
language English
publishDate 2025-05-01
publisher MDPI AG
record_format Article
series Chemosensors
spelling doaj-art-fe79cce4897b4d489cec383d275ff1d92025-08-20T03:14:32ZengMDPI AGChemosensors2227-90402025-05-0113516610.3390/chemosensors13050166Discovery of Lithospermate B as a Potential Ligand for the Malarial E2 Ubiquitin-Conjugating Enzyme via Multiplexed Native Mass SpectrometryJianying Han0Wesley C. Van Voorhis1Ronald J. Quinn2Miaomiao Liu3Institute for Biomedicine and Glycomics, Griffith University, Brisbane, QLD 4111, AustraliaCenter for Emerging and Re-emerging Infectious Diseases, Department of Medicine, University of Washington School of Medicine, MS 358061, 750 Republican St., Seattle, WA 98109-4766, USAInstitute for Biomedicine and Glycomics, Griffith University, Brisbane, QLD 4111, AustraliaInstitute for Biomedicine and Glycomics, Griffith University, Brisbane, QLD 4111, AustraliaThere is an urgent need for novel therapeutics to combat <i>Plasmodium falciparum</i>, especially in light of increasing drug resistance. Here, we present a multiplexed native mass spectrometry (MS) platform capable of simultaneously screening multiple protein targets against chemically diverse crude extracts with minimal sample preparation. A mixture of seven malarial proteins was analyzed under optimized native MS conditions, enabling the detection of specific ligand binding events. Using this platform, lithospermate B from <i>Salvia miltiorrhiza</i> (Danshen) was identified as a novel ligand for a malarial ubiquitin-conjugating enzyme with moderate affinity (Kd = 30.5 ± 2.5 μM). This is the first report linking lithospermate B to a malarial protein target, highlighting the potential of native MS to uncover new bioactivities of known natural products. This approach significantly enhances the throughput of protein–ligand screening and offers a powerful tool for early-stage natural product-based drug discovery.https://www.mdpi.com/2227-9040/13/5/166native mass spectrometrylithospermate Bubiquitin-conjugating enzyme<i>Salvia miltiorrhiza</i>
spellingShingle Jianying Han
Wesley C. Van Voorhis
Ronald J. Quinn
Miaomiao Liu
Discovery of Lithospermate B as a Potential Ligand for the Malarial E2 Ubiquitin-Conjugating Enzyme via Multiplexed Native Mass Spectrometry
Chemosensors
native mass spectrometry
lithospermate B
ubiquitin-conjugating enzyme
<i>Salvia miltiorrhiza</i>
title Discovery of Lithospermate B as a Potential Ligand for the Malarial E2 Ubiquitin-Conjugating Enzyme via Multiplexed Native Mass Spectrometry
title_full Discovery of Lithospermate B as a Potential Ligand for the Malarial E2 Ubiquitin-Conjugating Enzyme via Multiplexed Native Mass Spectrometry
title_fullStr Discovery of Lithospermate B as a Potential Ligand for the Malarial E2 Ubiquitin-Conjugating Enzyme via Multiplexed Native Mass Spectrometry
title_full_unstemmed Discovery of Lithospermate B as a Potential Ligand for the Malarial E2 Ubiquitin-Conjugating Enzyme via Multiplexed Native Mass Spectrometry
title_short Discovery of Lithospermate B as a Potential Ligand for the Malarial E2 Ubiquitin-Conjugating Enzyme via Multiplexed Native Mass Spectrometry
title_sort discovery of lithospermate b as a potential ligand for the malarial e2 ubiquitin conjugating enzyme via multiplexed native mass spectrometry
topic native mass spectrometry
lithospermate B
ubiquitin-conjugating enzyme
<i>Salvia miltiorrhiza</i>
url https://www.mdpi.com/2227-9040/13/5/166
work_keys_str_mv AT jianyinghan discoveryoflithospermatebasapotentialligandforthemalariale2ubiquitinconjugatingenzymeviamultiplexednativemassspectrometry
AT wesleycvanvoorhis discoveryoflithospermatebasapotentialligandforthemalariale2ubiquitinconjugatingenzymeviamultiplexednativemassspectrometry
AT ronaldjquinn discoveryoflithospermatebasapotentialligandforthemalariale2ubiquitinconjugatingenzymeviamultiplexednativemassspectrometry
AT miaomiaoliu discoveryoflithospermatebasapotentialligandforthemalariale2ubiquitinconjugatingenzymeviamultiplexednativemassspectrometry