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Articles by Suzanne Ackloo
Structure-based discovery of inhibitors of Mac1 domain of nonstructural protein-3 of SARS-CoV-2 by machine learning-augmented screening of chemical space
Abstract Significant efforts have been recently dedicated to the discovery of small molecule inhibitors against the Macrodomain 1 (Mac1) of nonstructural protein 3 (NSP3) as potential antivirals for SARS-CoV-2. Thus, Mac1 has also been selected as the target for the Critical Assessment of Hit-finding Experiments (CACHE) challenge #3.
Site-Specific Hydrogen–Deuterium Exchange Mass Spectrometry for Deep Explorations of Dynamic Shifts in Protein–Drug Interactions Click to copy article link Article link copied!
Introduction Click to copy section linkSection link copied! In biochemistry, Hydrogen–Deuterium eXchange (HDX) is a protein structure and dynamics-sensitive labeling technique where labile hydrogens exchange with deuterons from solvent upon dilution into D 2 O. (1,2) At physiological pH, amides from the peptide backbone exchange on a time scale from ms to days depending on the extent of their involvement in hydrogen bonding and/or solvent accessibility.
CACHE Challenge #3: Targeting the Nsp3 Macrodomain of SARS-CoV-2
Journal of Chemical Information and Modeling Cite this: J. Chem. Inf. Model. 2026, XXXX, XXX Click to copy citationCitation copied! . This publication is licensed under CC-BY 4.0 . You are free to share (copy and redistribute) this article in any medium or format and to adapt (remix, transform, and build upon) the material for any purpose, even commercially within the parameters below: Creative Commons (CC): This is a Creative Commons license. Attribution (BY): Credit must be given to the creator.
Enantioselective protein affinity selection mass spectrometry (E-ASMS) - Nature Communications
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Abstract We report an enantioselective protein affinity selection mass spectrometry screening approach (E-ASMS) that enables the detection of weak binders, informs on selectivity, and generates orthogonal confirmation of binding. After method development with control proteins, we screen 31 human proteins against a designed library of 8,217 chiral compounds.
By Xiaoyun Wang, Jianxian Sun, Shabbir Ahmad, Conrad V. Simoben, Stuart Green Verified, Madhushika Silva, Elisa Gibson, Danai Mavridi, Christopher G. Lenz, Andreas C. Joerger, Wyatt W. Yue, Tyler S Beyett, Susanne Müller, Stefan Knapp, Dafydd Owen, Rachel Harding, Matthieu Schapira, Peter Brown, Vijayaratnam Santhakumar, Suzanne Ackloo, Cheryl H Arrowsmith, Aled Edwards, Hui Peng
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Nature
Verified
OICR-41103 as a chemical probe for the DCAF1 WD40 domain - Communications Biology
Abstract Human DCAF1 is a multidomain protein that plays a critical role in protein homeostasis. Its WDR domain functions as a substrate recruitment module for RING-type CRL4 and HECT family EDVP E3 ubiquitin ligases, enabling the ubiquitination and proteasomal degradation of specific substrates. DCAF1’s activity has been implicated in cell proliferation and is documented to promote tumorigenesis.
Potent and selective SETDB1 covalent negative allosteric modulator reduces methyltransferase activity in cells - Nature Communications
Abstract A promising drug target, SETDB1, is a dual methyl-lysine (Kme) reader and methyltransferase implicated in cancer and neurodegenerative disease progression. To help understand the role of the triple Tudor domain (3TD) of SETDB1, its Kme reader, we first identify a low micromolar potency small molecule ligand, UNC6535, which occupies simultaneously both the TD2 and TD3 reader binding sites.
Crystal structures of DCAF1-PROTAC-WDR5 ternary complexes provide insight into DCAF1 substrate specificity - Nature Communications
Abstract Proteolysis-targeting chimeras (PROTACs) have been explored for the degradation of drug targets for more than two decades. However, only a handful of E3 ligase substrate receptors have been efficiently used. Downregulation and mutation of these receptors would reduce the effectiveness of such PROTACs. We recently developed potent ligands for DCAF1, a substrate receptor of EDVP and CUL4 E3 ligases.
A Target Class Ligandability Evaluation of WD40 Repeat-Containing Proteins
Introduction Click to copy section linkSection link copied! WD40 Repeat (WDR) proteins comprise one of the largest protein families, with ∼349 WDR encoding genes in the human genome. WDRs are generally understudied (Figure S1a, Table S1) though many have strong genetic links to human diseases and are involved in a wide variety of cellular processes including epigenetics, ubiquitin signaling, DNA repair, RNA splicing, and immune system signaling.
A host defense peptide mimetic, brilacidin, potentiates caspofungin antifungal activity against human pathogenic fungi - Nature Communications
Abstract Fungal infections cause more than 1.5 million deaths a year. Due to emerging antifungal drug resistance, novel strategies are urgently needed to combat life-threatening fungal diseases. Here, we identify the host defense peptide mimetic, brilacidin (BRI) as a synergizer with caspofungin (CAS) against CAS-sensitive and CAS-resistant isolates of Aspergillus fumigatus, Candida albicans, C. auris, and CAS-intrinsically resistant Cryptococcus neoformans. BRI also potentiates azoles against A.
Design and characterization of mutant and wildtype huntingtin proteins produced from a toolkit of scalable eukaryotic expression systems
Rachel J. Harding‡1, Peter Loppnau‡, Suzanne Ackloo‡, Alexander Lemak§, Ashley Hutchinson‡, Brittany Hunt‡2, Alex S. Holehouse¶3, Jolene C. Ho‡, Lixin Fan‖, Leticia Toledo-Sherman**4, Alma Seitova‡ and Cheryl H.
Design and characterization of mutant and wild-type huntingtin proteins produced from a toolkit of scalable eukaryotic expression systems
Author contributions: R.J.H. conceptualization; R.J.H., L.T.-S., and C.H.A. supervision; R.J.H. and C.H.A. funding acquisition; R.J.H., P.L., S.A., A.L., A.H., B.H., A.S.H., J.C.H., L.F., and A.S. investigation; R.J.H., P.L., S.A., A.L., A.S., and C.H.A. methodology; R.J.H., P.L., S.A., A.L., A.S.H., J.C.H., and A.S. writing-original draft; R.J.H. and C.H.A. project administration; R.J.H., P.L., S.A., A.L., A.H., B.H., A.S.H., J.C.H., L.F., L.T.-S., A.S., and C.H.A. writing-review and...
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