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sanguinarine
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2025 · IF 8.5

Sanguinarine induces the unfolding of Staphylococcus aureus-derived FtsZ and reduces the conformational flexibility necessary for assembly

Qiang Ma,Meinuo Chen,Zhimeng Zhang,Jianuo Cen,Shiqi Chen,Qiqi Wang,Ke Han,Zhiyue Feng,Congming Wu,Chongshan Dai,Yougang Zhong,Sihan Wang,Haiyang Jiang

Methicillin-resistant Staphylococcus aureus (MRSA) represents a serious global health challenge due to its resistance to multiple antibiotics, especially β-lactams, which limits treatment options and results in high morbidity and mortality rates. Thus, there is an urgent need for effective antibacterial agents and a deeper understanding of their mechanisms of action to combat the increasingly severe threat of bacterial resistance. In this study we have performed microbiological, molecular biology experiments and molecular dynamics simulations to investigate the antimicrobial efficacy of the sanguinarine (SAN) against MRSA and its conformational modulation of the Filamentous temperature-sensitive mutant Z (FtsZ). Our findings indicate that SAN exhibits promising anti-MRSA activity and spontaneously targets the nucleoid binding domain (NBD) of SaFtsZ to inhibit bacterial division. Additionally, SAN induces multiple single-nucleotide polymorphisms (SNPs) in the SaFtsZ coding gene, including Asp187, and site-directed mutagenesis confirms the critical role of this residue in binding. Notably, SAN causes the unfolding of SaFtsZ, significantly reducing the structural flexibility required for polymerization and triggering conformational changes. At higher dimensions, SAN disrupts protofilaments assembly, ultimately inhibiting septum formation and division. These findings provide multidimensional, high-resolution insights into the interaction between SAN and SaFtsZ, offering effective strategies for the prevention and eradication of MRSA.

CAS / MDL: 890764-63-3
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JOURNAL OF INDUSTRIAL AND ENGINEERING CHEMISTRY · 2018 · IF 4.841

Synthesis and characterization of magnetic molecularly imprinted polymers for enrichment of sanguinarine from the extraction wastewater of M. cordata

Ming Zhong,Yan-Hong Wang,Lu Wang,Rui-Qing Long,Chun-Lin Chen

A novel and efficient pretreatment method is proposed for the enrichment of sanguinarine (SA) from the extraction wastewater of Macleaya cordata (Willd) R. Br. using magnetic molecularly imprinted polymers (MMIPs) as solid phase adsorbent. The obtained MMIPs were synthesized by molecular imprinted technology and were well characterized with TEM, FT-IR, XRD, TGA, and VSM. The adsorption capacity and selectivity of MMIPs were also investigated. The results showed that the obtained MMIPs were core–shell spherical morphologies with an average diameter of 300   nm. The adsorption experiments showed that the MMIPs exhibited an almost three times higher adsorption capacity towards SA ( Q max   =   12.24   mg/g) than magnetic molecularly non-imprinted polymers (MNIPs) ( Q max   =   4.15   mg/g). The calculated parameters of adsorption isotherms and kinetics suggested that the adsorption process matched the Langmuir adsorption isotherm and pseudo-second-order kinetics model. The thermodynamic parameters were calculated, indicating that the adsorption process was spontaneous (ΔG 298K   =   −3.24   kJ/mol). The selectivity experiment showed that the MMIPs displayed higher selective adsorption capacity for SA compared to its reference compounds. Moreover, the MMIPs were applied to enrich SA from the extraction wastewater of M. cordata . The proposed method could provide an effective, simple and environmentally friendly way to identify and enrich SA from the extraction wastewater of M. cordata .

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Journal of Biomaterials and Tissue Engineering · 2022 ·Vol. 12 ·期 9 ·1699-1707 · IF 0.144

Application of Central Composite Design-Based Response Surface Methodology in Optimization of the Preparation Process of Sanguinarine Chitosan Microspheres

Li Chunmei,Ji Yubin,Li Wenlan

We designed the present experiment to prepare the sanguinarine chitosan microspheres. First, using the chitosan as a carrier, we prepared sanguinarine microspheres by emulsion cross-linking method, and determined the drug loading and encapsulation efficiency of sanguinarine microspheres by high performance liquid chromatography (HPLC). Then, taking the particle size as the evaluation indicator, we optimized the preparation process by the central composite design-based response surface methodology (CCD-based RSM). Finally, we performed in vitro release test to examine the cumulative release of sanguinarine microspheres. As a result, the optimal process conditions: 0.06 g for sanguinarine dosage, 0.07 g for chitosan dosage, 2% for acetic acid concentration, 3:10 for volume ratio of oil to water, 40 °C for emulsion cross-linking temperature, 500 r/min for rotation speed, and 5% for emulsifier dosage. Under such conditions, the sanguinarine microspheres had round shape, the average particle size was (8.14±0.13) μm, the particle size distribution was 2–20 μm, the drug loading was (4.58±0.93)%, and the encapsulation efficiency was (54.64±0.39)%, the cumulative release within 24 h was (78.34±1.08)%. In conclusion, we successfully prepared the sanguinarine chitosan microspheres, and they have excellent morphology, suitable particle size, and good sustained-release effect.

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JOURNAL OF CONTROLLED RELEASE · 2024 · IF 10.5

Fluorinated chitosan mediated transepithelial delivery of sanguinarine-loaded platinum (IV) prodrug for intravesical instillation therapy of muscle-invasive bladder cancer

Xinzi Hu,Guangzhi Li,Chenfan Kong,Lisha Liu,Dashi Deng,Guizhong Xin,Jian Pan,Song Wu,Qifang Lei

Cisplatin-based neoadjuvant chemotherapy is first-line strategy to inhibit progression and metastasis of muscle-invasive bladder cancer (MIBC). However, its clinical efficacy is often limited by drug resistance and severe systemic side effects, highlighting the urgent need for innovative therapeutic approaches. Despite advancements in cisplatin-based regimens, research on intravesical cisplatin delivery systems remains scarce. In this study, we developed an amphiphilic platinum(IV) prodrug micellar platform (Pt (IV)-DI-PEG) capable of efficiently encapsulating sanguinarine (San), which was further coated with fluorinated chitosan (FCS) to construct San@Pt(IV)-DI-PEG@FCS nanoparticles (SPFNPs) for intravesical instillation even targeting MIBC. The resulting SPFNPs demonstrated several advantages: the FCS coating facilitated enhanced trans-epithelial drug delivery by regulating bladder epithelial tight junction proteins, enabling efficient intravesical administration; Second, the glutathione (GSH)-responsive reduction of the Pt(IV) prodrug promoted tumor-targeted release of San and localized accumulation of Pt(II), while simultaneously depleting intracellular GSH. Furthermore, the released San induced reactive oxygen species (ROS) production, oxidative cleavage and inhibit the activation and function of poly (ADP-ribose) polymerase, collectively impairing nucleotide-excision repair and preventing the elimination of Pt-DNA adducts, resulting in persistent DNA damage, cell cycle arrest, and apoptosis in tumor cells. The synergistic effects of San and cisplatin were validated in both orthotopic mouse models and patient-derived orthotopic xenograft, demonstrating robust anti-tumor efficacy. This study underscores the potential of intravesical cisplatin formulations as a promising strategy for MIBC treatment, offering a shift from traditional systemic chemotherapy towards localized, targeted drug delivery systems.

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JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY · 2014 · IF 2.291

Competitive binding assay for G-quadruplex DNA and sanguinarine based on room temperature phosphorescence of Mn-doped ZnS quantum dots

Li-Na Wen,Meng-Xia Xie

s G-quadruplex DNA is an effective target for anticancer drug, and investigation of the G-quadruplex DNA with natural compounds plays a key role in the development of anticancer drugs. In this article, room temperature phosphorescence sensing system based on l -cysteine-capped Mn-doped ZnS QDs has been established. Sanguinarine can adsorb on the surface of Mn-doped QDs and quenched the phosphorescence emission of the sensor. When the G-quadruplex sequences combined with the sanguinarine of the QDs-sanguinarine system, the phosphorescence intensities of the QDs sensors would be restored, and the binding abilities of the G-quadruplex DNA with the sanguinarine can be evaluated by the phosphorescence recoveries of the sensor system. Based on the developed approach, the interaction of sanguinarine and six G-quadruplex DNA with various sequences (tel24-1, tel24-2, tel22, k-ras, HIF-1α and c-kit1) has been investigated. The results showed that the binding abilities of the G-quadruplex DNA with sanguinarine were related to their number of bases and conformations. The conformational changes of the six G-quadruplex DNA, after binding with sanguinarine, have also been probed by circular dichroism. Combining the changes of the phosphorescence lifetime, the binding mechanism of the G-quadruplex DNA and sanguinarine has been discussed. The developed method was simple, rapid and specific, and can avoid fluorescence interferences of the system, and it would be prospective to evaluate the interaction of the drug with different G-quadruplexes.

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Experimental and Therapeutic Medicine · 2026 ·Vol. 32 ·期 4 ·1-10 · IF 2.2

Sanguinarine chloride inducing ferroptosis and downregulating GPX4 expression in liver cancer: An integrated in silico, in vitro and in vivo study

Wen Ouyang,Jianxin Gao,Jing Liu,Lulu Qin,Bang Liu,Ying He,Dai Zhou

Experimental and Therapeutic Medicine is an international journal devoted to laboratory and clinical medicine.

CAS / MDL: 5578-73-4
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INTERNATIONAL IMMUNOPHARMACOLOGY · 2026 · IF 5.6

Characterization of a novel porcine circovirus type 2a sequence and anti-viral evaluation of matrine and sanguinarine combined with network pharmacology and molecular docking

Wen-Ting Qiao,Xin Yao,Wei-Hong Lu,Yu-Qian Zhang,Bin Zhou,Jin-Long Li

Novel PCV2a isolate carries KATALT→KVPAQT mutation in neutralizing epitope. • Mutant epitope shows reduced antibody binding (89.4% → 40.3% inhibition). • Matrine and sanguinarine inhibit PCV2 in vitro and in silico. Porcine circovirus type 2 (PCV2) remains an economically significant pathogen affecting global swine herds, with emerging genetic variants raising concerns about potential immune escape from existing PCV2a-based vaccines. In this study, we identified a novel PCV2a isolate carrying four nonsynonymous substitutions (S68A, M131T, V133A, and K191A) in the capsid (Cap) protein, with the M131T/V133A substitutions located within the well-characterized conformational neutralizing epitope at residues 132–137 (KATALT→KVPAQT). To assess the functional impact of this mutation on antibody recognition, we developed a liquid-phase competitive ELISA using synthetic peptides representing the wild-type (WT) and mutant epitope sequences, together with PCV2-positive reference serum. The WT peptide effectively competed for antibody binding (inhibition rate 89.40%), whereas the mutant peptide exhibited a markedly reduced inhibition rate (40.28%), indicating impaired antibody recognition at this epitope. Combined with three-dimensional structural modeling showing altered surface charge and spatial conformation within the epitope region, these findings provide direct evidence that the KVPAQT mutation reduces neutralizing antibody binding to this critical epitope. Network pharmacology and molecular docking were then applied to assess matrine and sanguinarine targeting the mutant Cap protein. Both compounds exhibited strong binding affinities, with binding energies of −8.2 and − 7.9 kcal/mol for matrine and sanguinarine, respectively. Furthermore, in vitro antiviral assays demonstrated that both compounds effectively suppressed PCV2 replication in PK-15 cells. Overall, these findings define a clinically isolated PCV2a antigenic variant with impaired antibody recognition and establish an integrated computational–experimental platform for efficiently screening natural products against emerging PCV2 variants. This study provides a molecular basis for understanding PCV2 antigenic drift and a practical strategy for antiviral development.

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