Peptide inhibitors of the Keap1–Nrf2 protein–protein interaction with improved binding and cellular activity

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Anti-inflammatory Effect of a Cell-Penetrating Peptide Targeting the Nrf2/Keap1 Interaction

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Design, Synthesis, and Evaluation of Triazole Derivatives That Induce Nrf2 Dependent Gene Products and Inhibit the Keap1–Nrf2 Protein–Protein Interaction

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Contribution of Nrf2 Modulation to the Mechanism of Action of Analgesic and Anti-inflammatory Drugs in Pre-clinical and Clinical Stages

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MOrPH-PhD: An Integrated Phage Display Platform for the Discovery of Functional Genetically Encoded Peptide Macrocycles

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Peptide and small molecule inhibitors of the Keap1–Nrf2 protein–protein interaction

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Molecular dynamics, quantum mechanics and docking studies of some Keap1 inhibitors – An insight into the atomistic mechanisms of their antioxidant potential

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Targeting Protein–Protein Interfaces with Peptides: The Contribution of Chemical Combinatorial Peptide Library Approaches

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Discovery of 2-oxy-2-phenylacetic acid substituted naphthalene sulfonamide derivatives as potent KEAP1-NRF2 protein-protein interaction inhibitors for inflammatory conditions

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Crystallography-Guided Optimizations of the Keap1–Nrf2 Inhibitors on the Solvent Exposed Region: From Symmetric to Asymmetric Naphthalenesulfonamides

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Identification of novel Nrf2 activators from Cinnamomum chartophyllum H.W. Li and their potential application of preventing oxidative insults in human lung epithelial cells

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Inhibiting the Keap1/Nrf2 Protein‐Protein Interaction with Protein‐Like Polymers

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Fragment-growing guided design of Keap1-Nrf2 protein-protein interaction inhibitors for targeting myocarditis

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Buyang Huanwu decoction alleviates oxidative injury of cerebral ischemia-reperfusion through PKCε/Nrf2 signaling pathway

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Polar Recognition Group Study of Keap1-Nrf2 Protein–Protein Interaction Inhibitors

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Development of a steady‐state FRET‐based assay to identify inhibitors of the Keap1‐Nrf2 protein–protein interaction

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Identification of compounds that inhibit the binding of Keap1a/Keap1b Kelch DGR domain with Nrf2 ETGE/DLG motifs in zebrafish

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Novel diterpenoid-type activators of the Keap1/Nrf2/ARE signaling pathway and their regulation of redox homeostasis

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New strategies to inhibit KEAP1 and the Cul3-based E3 ubiquitin ligases

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PinaColada: peptide–inhibitor ant colony ad-hoc design algorithm

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Perfluoroarene-based peptide macrocycles that inhibit the Nrf2/Keap1 interaction

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Phenyl Bis-Sulfonamide Keap1-Nrf2 Protein–Protein Interaction Inhibitors with an Alternative Binding Mode

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Perspectives on the Clinical Development of NRF2-Targeting Drugs

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Advances in KEAP1-based PROTACs as emerging therapeutic modalities: Structural basis and progress

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Engineering a genetically encoded competitive inhibitor of the KEAP1–NRF2 interaction via structure-based design and phage display

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Dual-functional alginate crosslinker: Independent control of crosslinking density and cell adhesive properties of hydrogels via separate conjugation pathways

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A phage display-based strategy for the de novo creation of disulfide-constrained and isomer-free bicyclic peptide affinity reagents

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An Integrated Molecular Grafting Approach for the Design of Keap1-Targeted Peptide Inhibitors

Yin, H., Huang, Y., Best, S. A., Sutherland, K. D., Craik, D. J., & Wang, C. K. L. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00388 · Cited by 19 · see citing works

Rational cyclization-based minimization of entropy penalty upon the binding of Nrf2-derived linear peptides to Keap1: A new strategy to improve therapeutic peptide activity against sepsis

Chen, K., Huang, L., & Shen, B. (2018) · Biophysical Chemistry · doi:10.1016/j.bpc.2018.11.002 · Cited by 19 · see citing works

Computational Prediction of Cyclic Peptide Structural Ensembles and Application to the Design of Keap1 Binders

Lopez, F., Miao, J., Damjanovic, J., Bischof, L., Braun, M. B., Ling, Y., Hartmann, M. D., Lin, Y., & Kritzer, J. A. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01337 · Cited by 17 · see citing works

Bis-Michael Acceptors as Novel Probes to Study the Keap1/Nrf2/ARE Pathway

Deny, L. J., Traboulsi, H., Cantin, A. M., Marsault, É., Richter, M. V., & Bélanger, G. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01132 · Cited by 17 · see citing works

Exploring new strategies for grafting binding peptides onto protein loops using a consensus‐designed tetratricopeptide repeat scaffold

Madden, S. K., Perez‐Riba, A., & Itzhaki, L. S. (2019) · Protein Science · doi:10.1002/pro.3586 · Cited by 17 · see citing works

Noncellular screening for the discovery of protein–protein interaction modulators

Kieffer, C., Jourdan, J., Jouanne, M., & Voisin‐Chiret, A. S. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.07.012 · Cited by 17 · see citing works

Fast and Selective Reaction of 2-Benzylacrylaldehyde with 1,2-Aminothiol for Stable N-Terminal Cysteine Modification and Peptide Cyclization

Wu, Y., Li, C., Fan, S., Zhao, Y., & Wu, C. (2021) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.1c00378 · Cited by 16 · see citing works

Pharmacological characterization of a novel peptide inhibitor of the Keap1-Nrf2 protein-protein interaction

Aparici, M., Bravo, M., Calama, E., García‐González, V., Domènech, T., Córdoba, M., Roger, I., Cortijo, J., Góngora‐Benítez, M., Paradís‐Bas, M., et al. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115226 · Cited by 15 · see citing works

Targeting kelch-like (KLHL) proteins: achievements, challenges and perspectives

Zhou, Y., Zhang, Q., Zhao, Z., Hu, X., You, Q., & Jiang, Z. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116270 · Cited by 14 · see citing works

Targeting Oxidative Stress in Stroke

Bach, A. (2017) · Springer series in translational stroke research · doi:10.1007/978-3-319-45345-3_8 · Cited by 15 · see citing works

Structural basis of Nrf2 activation by flavonolignans from silymarin

Bello, M. (2022) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2022.108393 · Cited by 10 · see citing works

Cyclo(-Phe-Phe) alleviates chick embryo liver injury via activating the Nrf2 pathway

Zhang, Q., Han, S., Huang, R.-P., Jiang, M.-Y., Yan, C., Li, X.-Y., Zhan, Y.-J., Li, X., Li, Y.-F., Kurihara, H., et al. (2022) · Food & Function · doi:10.1039/d2fo00674j · Cited by 10 · see citing works

Peptide Macrocycles Developed from Precisely Regulated Multiple Cyclization of Unprotected Peptides

Wang, J., Zha, M., Fei, Q., Liu, W., Zhao, Y., & Wu, C. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201703139 · Cited by 9 · see citing works

Development of Keap1-interactive small molecules that regulate Nrf2 transcriptional activity

Georgakopoulos, N., Gatliff, J., & Wells, G. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.08.002 · Cited by 8 · see citing works

Selection and evolution of disulfide-rich peptides via cellular protein quality control

Meng, X., Xu, C., Fan, S., Meng, D., Zhuang, J., Duan, Z., Zhao, Y., & Wu, C. (2023) · Chemical Science · doi:10.1039/d2sc05343h · Cited by 7 · see citing works

Solid-Phase Synthesis of Triostin A Using a Symmetrical Bis(diphenylmethyl) Linker System

Sable, G. A., & Lim, D. (2015) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.5b01055 · Cited by 7 · see citing works

Structural investigation of Keap1–Nrf2 protein–protein interaction (PPI) inhibitors for treating myocarditis through molecular simulations

Tuo, Y., Tang, Y., Yu, Y., Liang, H., Huang, B., Geng, S., & Wang, Y. (2023) · New Journal of Chemistry · doi:10.1039/d2nj03078k · Cited by 6 · see citing works

Design and Synthesis of Cross-Link-Dense Peptides by Manipulating Regioselective Bisthioether Cross-Linking and Orthogonal Disulfide Pairing

Dong, H., Meng, X., Zheng, X., Cheng, X., Zheng, Y., Zhao, Y., & Wu, C. (2019) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.9b00164 · Cited by 6 · see citing works

The Dual Role of Nrf2 Signaling in Virus Infections: Antiviral Guardian or Proviral Accomplice?

Sahoo, B. R., Pandey, K. K., & Pattnaik, A. K. (2025) · Pathogens · doi:10.3390/pathogens15010008 · Cited by 2 · see citing works

Protein-Peptide Interaction Design: PepCrawler and PinaColada

Zaidman, D., & Wolfson, H. J. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6798-8_16 · Cited by 2 · see citing works

PROTEIN-PROTEIN INTERACTION ANALYSIS TO IDENTIFY NUCLEAR FACTOR-ERYTHROID-2 FACTOR 2 (NRF2) INHIBITION BY EXTRACELLULAR ENZYMES FROM WATER KEFIR ORGANISMS

Aligita, W., Singgih, M., Sutrisno, E., & Adnyana, I. K. (2023) · International Journal of Applied Pharmaceutics · doi:10.22159/ijap.2023.v15s2.20 · Cited by 1 · see citing works

Tetrazole-containing naphthalene bis-sulfonamide Keap1-Nrf2 interaction inhibitors with unexpected binding modes

Georgakopoulos, N., Talapatra, S. K., Naidu, S. D., Dikovskaya, D., Higgins, M., Gatliff, J., Nikoloudaki, R., Schaap, M., Walker, J. M., Wardby, C., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103924 · Cited by 1 · see citing works

Discovery and Development of Keap1-Nrf2 Protein-Protein Interaction Inhibitors

Jiang, Z., & You, Q. (2018) · Springer eBooks · doi:10.1007/978-981-13-0773-7_10 · Cited by 1 · see citing works

Small-Molecule Inhibitors of Protein–Protein Interactions as Therapeutics

Poluri, K. M., Gulati, K., Tripathi, D. K., & Nagar, N. (2023) · Springer eBooks · doi:10.1007/978-981-99-2423-3_7 · Cited by 1 · see citing works

Targeting Selective Autophagy of Insoluble Protein Aggregates

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801944-3.00005-9

FAIR and bias-free network modules for mechanism-based disease redefinitions

Hassan, A. (2021) · doi:10.26481/dis.20210707ah

Protein-protein interaction inhibitors in cancer

Hardcastle, I. R., Goujon-Ricci, J., & Thompson, W. I. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00067-4

Preparation, Peptidomic Characterization, and Molecular Docking Analysis of Antioxidant Peptides Derived From Cottonseed Protein Concentrate

Chen, J., Amuti, A., Wei, C., Zhao, Y., Liu, W., 罗鹏, & Zhao, Q. (2026) · Journal of Food Process Engineering · doi:10.1111/jfpe.70832

BindingDB Entry 50011439: Design, Synthesis, and Structure-Activity Relationships of Indoline-Based Kelch-like ECH-Associated Protein 1-Nuclear Factor (Erythroid-Derived 2)-Like 2 (Keap1-Nrf2) Protein-Protein Interaction Inhibitors.

BindingDB (2022) · UC San Diego · doi:10.7270/q2vd7329

BindingDB Entry 50017940: TBA

BindingDB (2023) · UC San Diego · doi:10.7270/q2q52trd

BindingDB Entry 50046585: Design, Synthesis, and Evaluation of Triazole Derivatives That Induce Nrf2 Dependent Gene Products and Inhibit the Keap1-Nrf2 Protein-Protein Interaction.

BindingDB (2016) · UC San Diego · doi:10.7270/q2fn181b

BindingDB Entry 50001714: Non-covalent Small-Molecule Kelch-like ECH-Associated Protein 1-Nuclear Factor Erythroid 2-Related Factor 2 (Keap1-Nrf2) Inhibitors and Their Potential for Targeting Central Nervous System Diseases.

BindingDB (2020) · UC San Diego · doi:10.7270/q2cj8h17

BindingDB Entry 50006254: Non-electrophilic modulators of the canonical Keap1/Nrf2 pathway.

BindingDB (2020) · UC San Diego · doi:10.7270/q20v8gsc

BindingDB Entry 50022106: Targeting kelch-like (KLHL) proteins: achievements, challenges and perspectives.

BindingDB (2025) · UC San Diego · doi:10.7270/q29028gr

BindingDB Entry 50012263: Discovery of 2-oxy-2-phenylacetic acid substituted naphthalene sulfonamide derivatives as potent KEAP1-NRF2 protein-protein interaction inhibitors for inflammatory conditions.

BindingDB (2022) · UC San Diego · doi:10.7270/q2fj2mgn

BindingDB Entry 50017885: Phenyl Bis-Sulfonamide Keap1-Nrf2 Protein-Protein Interaction Inhibitors with an Alternative Binding Mode.

BindingDB (2023) · UC San Diego · doi:10.7270/q2t157qm

BindingDB Entry 50011387: Optimization of linear and cyclic peptide inhibitors of KEAP1-NRF2 protein-protein interaction.

BindingDB (2022) · UC San Diego · doi:10.7270/q2qv3r4s

BindingDB Entry 50001541: Discovery of a head-to-tail cyclic peptide as the Keap1-Nrf2 protein-protein interaction inhibitor with high cell potency.

BindingDB (2020) · UC San Diego · doi:10.7270/q2pk0jnt

The discovery and evaluation of inhibitors of the KEAP1-NRF2 protein-protein interaction

Hancock, R. (2013) · UCL Discovery (University College London)

Modified Peptide Inhibitors of the Keap1–Nrf2 Protein–Protein Interaction Incorporating Unnatural Amino Acids

Georgakopoulos, N., Talapatra, S. K., Gatliff, J., Kozielski, F., & Wells, G. (2018) · ChemBioChem · doi:10.1002/cbic.201800170 · Cited by 40 · see citing works

Peptide inhibitors of the Keap1–Nrf2 protein–protein interaction

Hancock, R., Bertrand, H. C., Tsujita, T., Naz, S., El-Bakry, A., Laoruchupong, J., Hayes, J. D., & Wells, G. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.486 · Cited by 147 · see citing works

Binding thermodynamics and kinetics guided optimization of potent Keap1–Nrf2 peptide inhibitors

Lu, M.-C., Chen, Z.-Y., Wang, Y.-L., Jiang, Y.-L., Yuan, Z.-W., You, Q.-D., & Jiang, Z.-Y. (2015) · RSC Advances · doi:10.1039/c5ra16262a · Cited by 55 · see citing works

Discovery of Potent Keap1–Nrf2 Protein–Protein Interaction Inhibitor Based on Molecular Binding Determinants Analysis

Jiang, Z., Lu, M., Xu, L., Yang, T., Xi, M., Xu, X., Guo, X., Zhang, X., You, Q., & Sun, H.-P. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5000529 · Cited by 263 · see citing works