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Dual-template epitope imprinted nanoparticles for anti-glycolytic tumor-targeted treatment.
J Colloid Interface Sci
December 2024
State Key Laboratory of Medicinal Chemical Biology, Tianjin Key Laboratory of Biosensing and Molecular Recognition, Research Center for Analytical Sciences, College of Chemistry, Nankai University, Tianjin 300071, China; National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China. Electronic address:
Glycolysis provides tumors with abundant nutrients through glucose (Glu) metabolism. As a therapeutic target, precise targeting and effective inhibition of the glycolysis process remains a major challenge in anti-metabolic therapy. In this study, a novel dual-template molecularly imprinted polymer (D-MIP), capable of specifically recognizing glucose transporter member 1 (GLUT1) and hexokinase-2 (HK2) was prepared for anti-glycolytic tumor therapy.
View Article and Find Full Text PDFUpdates on Intrinsic Medicinal Chemistry of 1,4-dihydropyridines, Perspectives on Synthesis and Pharmacokinetics of Novel 1,4-dihydropyrimidines as Calcium Channel Blockers: Clinical Pharmacology.
Curr Top Med Chem
January 2025
Department of Pharmaceutical Chemistry, JSS College of Pharmacy, JSS Academy of Higher Education & Research (JSS AHER), Mysuru, Karnataka, India.
Background: Several chemical studies described the physiological efficacy of 1,4- dihydropyridines (DHPs). DHPs bind to specific sites on the α1 subunit of L-type calcium channels, where they demonstrate a more pronounced inhibition of Ca2+ influx in vascular smooth muscle compared to myocardial tissue. This selective inhibition is the basis for their preferential vasodilatory action on peripheral and coronary arteries, a characteristic that underlies their therapeutic utility in managing hypertension and angina.
View Article and Find Full Text PDFDual-Enzyme-Instructed Peptide Self-Assembly to Boost Immunogenic Cell Death by Coordinating Intracellular Calcium Overload and Chemotherapy.
ACS Nano
January 2025
Zhejiang Key Laboratory of Intelligent Cancer Biomarker Discovery and Translation, The First Affiliated Hospital, Wenzhou Medical University, Wenzhou 325035, Zhejiang, P. R. China.
The concept of immunogenic cell death (ICD) induced by chemotherapy as a potential synergistic modality for cancer immunotherapy has been widely discussed. Unfortunately, most chemotherapeutic agents failed to dictate effective ICD responses due to their defects in inducing potent ICD signaling. Here, we report a dual-enzyme-instructed peptide self-assembly platform of (CPT-GFFpY-PLGVRK-Caps) that cooperatively utilizes camptothecin (CPT) and capsaicin (Caps) to promote ICD and engage systemic adaptive immunity for tumor rejection.
View Article and Find Full Text PDFUnveiling the mechanism of action of a novel natural dual inhibitor of SARS-CoV-2 Mpro and PLpro with molecular dynamics simulations.
Nat Prod Bioprospect
January 2025
Hubei Key Laboratory of Natural Medicinal Chemistry and Resource Evaluation, School of Pharmacy, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 430030, People's Republic of China.
In the twenty-first century, we have witnessed multiple coronavirus pandemics. Despite declining SARS-CoV-2 cases, continued research remains vital. We report the discovery of sydowiol B, a natural product, as a dual inhibitor of SARS-CoV-2 main protease (Mpro) and papain-like protease (PLpro).
View Article and Find Full Text PDFA propofol binding site in the voltage sensor domain mediates inhibition of HCN1 channel activity.
Sci Adv
January 2025
Department of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Article Synopsis
- HCN ion channels play a key role in cellular activity and pain perception, with propofol acting as an analgesic by inhibiting their function.
- Researchers used a propofol analog to pinpoint binding sites on the human HCN1 isoform, revealing a specific pocket formed by certain residues in the channel.
- Mutations in this binding pocket affect propofol's ability to modulate HCN1 currents, highlighting its specific binding mechanism and offering insights for developing targeted HCN channel modulators.
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