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1.
Mol Biol Rep ; 51(1): 722, 2024 Jun 03.
Article in English | MEDLINE | ID: mdl-38829419

ABSTRACT

BACKGROUND: Yersinia pestis is a bacterium that causes the disease plague. It has caused the deaths of many people throughout history. The bacterium possesses several virulence factors (pPla, pFra, and PYV). PFra plasmid encodes fraction 1 (F1) capsular antigen. F1 protein protects the bacterium against host immune cells through phagocytosis process. This protein is specific for Y. pestis. Many diagnostic techniques are based on molecular and serological detection and quantification of F1 protein in different food and clinical samples. Aptamers are small nucleic acid sequences that can act as specific ligands for many targets.This study, aimed to isolate the high-affinity ssDNA aptamers against F1 protein. METHODS AND RESULTS: In this study, SELEX was used as the main strategy in screening aptamers. Moreover, enzyme-linked aptamer sorbent assay (ELASA) and surface plasmon resonance (SPR) were used to determine the affinity and specificity of obtained aptamers to F1 protein. The analysis showed that among the obtained aptamers, the three aptamers of Yer 21, Yer 24, and Yer 25 were selected with a KD value of 1.344E - 7, 2.004E - 8, and 1.68E - 8 M, respectively. The limit of detection (LoD) was found to be 0.05, 0.076, and 0.033 µg/ml for Yer 21, Yer 24, and Yer 25, respectively. CONCLUSION: This study demonstrated that the synthesized aptamers could serve as effective tools for detecting and analyzing the F1 protein, indicating their potential value in future diagnostic applications.


Subject(s)
Aptamers, Nucleotide , Bacterial Proteins , SELEX Aptamer Technique , Yersinia pestis , Yersinia pestis/genetics , SELEX Aptamer Technique/methods , Bacterial Proteins/genetics , Surface Plasmon Resonance/methods , Humans , Plague/diagnosis , Plague/microbiology , Antigens, Bacterial
2.
Nat Commun ; 15(1): 4733, 2024 Jun 03.
Article in English | MEDLINE | ID: mdl-38830951

ABSTRACT

Polymyxins are gram-negative antibiotics that target lipid A, the conserved membrane anchor of lipopolysaccharide in the outer membrane. Despite their clinical importance, the molecular mechanisms underpinning polymyxin activity remain unresolved. Here, we use surface plasmon resonance to kinetically interrogate interactions between polymyxins and lipid A and derive a phenomenological model. Our analyses suggest a lipid A-catalyzed, three-state mechanism for polymyxins: transient binding, membrane insertion, and super-stoichiometric cluster accumulation with a long residence time. Accumulation also occurs for brevicidine, another lipid A-targeting antibacterial molecule. Lipid A modifications that impart polymyxin resistance and a non-bactericidal polymyxin derivative exhibit binding that does not evolve into long-lived species. We propose that transient binding to lipid A permeabilizes the outer membrane and cluster accumulation enables the bactericidal activity of polymyxins. These findings could establish a blueprint for discovery of lipid A-targeting antibiotics and provide a generalizable approach to study interactions with the gram-negative outer membrane.


Subject(s)
Anti-Bacterial Agents , Lipid A , Polymyxin B , Surface Plasmon Resonance , Polymyxin B/pharmacology , Polymyxin B/metabolism , Lipid A/metabolism , Lipid A/chemistry , Anti-Bacterial Agents/pharmacology , Anti-Bacterial Agents/chemistry , Anti-Bacterial Agents/metabolism , Microbial Sensitivity Tests , Bacterial Outer Membrane/metabolism , Bacterial Outer Membrane/drug effects , Kinetics
3.
Colloids Surf B Biointerfaces ; 238: 113923, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38692173

ABSTRACT

The rapid advancement of photodynamic therapy (PDT) antibacterial materials has led to promising alternatives to antibiotics for treating bacterial infections. However, antibacterial drugs have poor light absorption and utilization rates, which limits their practical application. Constructing two-dimensional (2D) heterojunctions from materials with matching photophysical properties has emerged as a highly effective strategy for achieving high-efficiency photo-antibacterial performance. Here, we designed and prepared an atom co-sharing Bi/Bi4O5Br2 nanosheet heterojunction by a simple in situ reduction. This heterojunction material combines outstanding biocompatibility with excellent bactericidal efficiency, which exceeded 90 % against Escherichia coli (a Gram-negative bacterium) and Staphylococcus aureus (a Gram-positive bacterium) under visible light irradiation, around nine-fold higher than that with pure Bi4O5Br2 nanosheets. The results suggest that localized surface plasmon resonance (LSPR) of shared Bi atoms on the Bi4O5Br2 nanosheets promotes light utilization and the separation and transfer of photo-generated charges, thus producing more abundant reactive oxygen species (ROS), which can partake in the PDT antibacterial effect. Our study underscores the potential utility of LSPR-enhanced Bi-based nanosheet heterojunctions for safe and efficient PDT to combat bacterial infections.


Subject(s)
Anti-Bacterial Agents , Bismuth , Escherichia coli , Light , Nanostructures , Staphylococcus aureus , Anti-Bacterial Agents/pharmacology , Anti-Bacterial Agents/chemistry , Escherichia coli/drug effects , Staphylococcus aureus/drug effects , Nanostructures/chemistry , Bismuth/chemistry , Bismuth/pharmacology , Catalysis , Microbial Sensitivity Tests , Photochemical Processes , Reactive Oxygen Species/metabolism , Surface Plasmon Resonance , Photochemotherapy , Particle Size
4.
Anal Chem ; 96(21): 8791-8799, 2024 May 28.
Article in English | MEDLINE | ID: mdl-38742926

ABSTRACT

MicroRNAs (miRNAs) are novel tumor biomarkers owing to their important physiological functions in cell communication and the progression of multiple diseases. Due to the small molecular weight, short sequence length, and low concentration levels of miRNA, miRNA detection presents substantial challenges, requiring the advancement of more refined and sensitive techniques. There is an urgent demand for the development of a rapid, user-friendly, and sensitive miRNA analysis method. Here, we developed an enhanced biotin-streptavidin dual-mode phase imaging surface plasmon resonance (PI-SPR) aptasensor for sensitive and rapid detection of miRNA. Initially, we evaluated the linear sensing range for miRNA detection across two distinct sensing modalities and investigated the physical factors that influence the sensing signal in the aptamer-miRNA interaction within the PI-SPR aptasensor. Then, an enhanced biotin-streptavidin amplification strategy was introduced in the PI-SPR aptasensor, which effectively reduced the nonspecific adsorption by 20% and improved the limit of detection by 548 times. Furthermore, we have produced three types of tumor marker chips, which utilize the rapid sensing mode (less than 2 min) of PI-SPR aptasensor to achieve simultaneous detection of multiple miRNA markers in the serum from clinical cancer patients. This work not only developed a new approach to detect miRNA in different application scenarios but also provided a new reference for the application of the biotin-streptavidin amplification system in the detection of other small biomolecules.


Subject(s)
Aptamers, Nucleotide , Biotin , MicroRNAs , Streptavidin , Surface Plasmon Resonance , MicroRNAs/analysis , MicroRNAs/blood , Biotin/chemistry , Surface Plasmon Resonance/methods , Streptavidin/chemistry , Humans , Aptamers, Nucleotide/chemistry , Limit of Detection , Biomarkers, Tumor/blood , Biomarkers, Tumor/analysis , Biosensing Techniques/methods
5.
Carbohydr Polym ; 337: 122137, 2024 Aug 01.
Article in English | MEDLINE | ID: mdl-38710567

ABSTRACT

Xylans' unique properties make it attractive for a variety of industries, including paper, food, and biochemical production. While for some applications the preservation of its natural structure is crucial, for others the degradation into monosaccharides is essential. For the complete breakdown, the use of several enzymes is required, due to its structural complexity. In fact, the specificity of enzymatically-catalyzed reactions is guided by the surface, limiting or regulating accessibility and serving structurally encoded input guiding the actions of the enzymes. Here, we investigate enzymes at surfaces rich in xylan using surface plasmon resonance spectroscopy. The influence of diffusion and changes in substrate morphology is studied via enzyme surface kinetics simulations, yielding reaction rates and constants. We propose kinetic models, which can be applied to the degradation of multilayer biopolymer films. The most advanced model was verified by its successful application to the degradation of a thin film of polyhydroxybutyrate treated with a polyhydroxybutyrate-depolymerase. The herein derived models can be employed to quantify the degradation kinetics of various enzymes on biopolymers in heterogeneous environments, often prevalent in industrial processes. The identification of key factors influencing reaction rates such as inhibition will contribute to the quantification of intricate dynamics in complex systems.


Subject(s)
Surface Plasmon Resonance , Xylans , Xylans/chemistry , Xylans/metabolism , Surface Plasmon Resonance/methods , Kinetics , Surface Properties
6.
J Agric Food Chem ; 72(19): 11259-11267, 2024 May 15.
Article in English | MEDLINE | ID: mdl-38691423

ABSTRACT

Peanut allergen monitoring is currently an effective strategy to avoid allergic diseases, while food matrix interference is a critical challenge during detection. Here, we developed an antifouling surface plasmon resonance sensor (SPR) with stratified zwitterionic peptides, which provides both excellent antifouling and sensing properties. The antifouling performance was measured by the SPR, which showed that stratified peptide coatings showed much better protein resistance, reaching ultralow adsorption levels (<5 ng/cm2). Atomic force microscopy was used to further analyze the antifouling mechanism from a mechanical perspective, which demonstrated lower adsorption forces on hybrid peptide coatings, confirming the better antifouling performance of stratified surfaces. Moreover, the recognition of peanut allergens in biscuits was performed using an SPR with high efficiency and appropriate recovery results (98.2-112%), which verified the feasibility of this assay. Therefore, the fabrication of antifouling sensors with stratified zwitterionic peptides provides an efficient strategy for food safety inspection.


Subject(s)
Allergens , Arachis , Peptides , Surface Plasmon Resonance , Surface Plasmon Resonance/methods , Arachis/chemistry , Arachis/immunology , Peptides/chemistry , Peptides/immunology , Allergens/analysis , Allergens/immunology , Allergens/chemistry , Biofouling/prevention & control , Food Contamination/analysis , Plant Proteins/immunology , Plant Proteins/chemistry , Plant Proteins/analysis , Biosensing Techniques/instrumentation , Biosensing Techniques/methods , Adsorption
7.
Mikrochim Acta ; 191(6): 335, 2024 05 17.
Article in English | MEDLINE | ID: mdl-38760484

ABSTRACT

The release of tire wear substances in the environment is raising concerns about potential impacts on aquatic ecosystems. The purpose of this study was to develop a quick and inexpensive screening test for the following tire wear substances: 6-phenylphenyldiamine quinone (6-PPD quinone), hexamethoxymethylmelamine (HMMM), 1-3-diphenylguanidine (1,3-DPG), and melamine. A dual strategy consisting of nanogold (nAu) signal intensity and the plasmonic ruler principle was used based on the spectral shift from the unaggregated free-form nAu from 525 nm to aggregated nAu at higher wavelengths. The shift in resonance corresponded to the relative sizes of the tire wear substances at the surface of nAu: 6-PPD (560 nm), HMMM (590 nm), 1,3-DPG (620 nm), and melamine (660 nm) in a concentration-dependent manner. When present in mixtures, a large indiscriminate band between 550 and 660 nm with a maximum corresponding to the mean intermolecular distance of 0.43 nm from the tested individual substances suggests that all compounds indiscriminately interacted at the surface of nAu. An internal calibration methodology was developed for mixtures and biological extracts from mussels and biofilms and revealed a proportional increase in absorbance at the corresponding resonance line for each test compound. Application of this simple and quick methodology revealed the increased presence of melamine and HMMM compounds in mussels and biofilms collected at urban sites (downstream city, road runoffs), respectively. The data also showed that treated municipal effluent decreased somewhat melamine levels in mussels.


Subject(s)
Gold , Metal Nanoparticles , Triazines , Gold/chemistry , Metal Nanoparticles/chemistry , Triazines/analysis , Triazines/chemistry , Surface Plasmon Resonance/methods , Water Pollutants, Chemical/analysis
8.
ACS Appl Mater Interfaces ; 16(20): 25879-25891, 2024 May 22.
Article in English | MEDLINE | ID: mdl-38718301

ABSTRACT

Biological imaging-guided targeted tumor therapy has been a soughtafter goal in the field of cancer diagnosis and treatment. To this end, we proposed a strategy to modulate surface plasmon resonance and endow WO3-x nanoparticles (NPs) with enzyme-like catalytic properties by doping Fe2+ in the structure of the NPs. Doping of the Fe2+ introduced oxygen vacancies into the structure of the NPs, inducing a red shift of the maximum absorption wavelength into the near-infrared II (NIR-II) region and enhancing the photoacoustic (PA) and photothermal properties of the NPs for more effective imaging-guided cancer therapy. Under NIR-II laser irradiation, the Fe-WO3-x NPs produced very strong NIR-II PA and photothermal effects, which significantly enhanced the PA imaging and photothermal treatment effects. On the other hand, Fe2+ in Fe-WO3-x could undergo Fenton reactions with H2O2 in the tumor tissue to generate ·OH for chemodynamic therapy. In addition, Fe-WO3-x can also catalyze the above reactions to produce more reactive oxygen species (ROS) and induce the oxidation of NADH to interfere with intracellular adenosine triphosphate (ATP) synthesis, thereby further improving the efficiency of cancer therapy. Specific imaging of tumor tissue and targeted synergistic therapy was achieved after ligation of a MUC1 aptamer to the surface of the Fe-WO3-x NPs by the complexing of -COOH in MUC1 with tungsten ions on the surface of the NPs. These results demonstrated that Fe-WO3-x NPs could be a promising diagnosis and therapeutic agent for cancer. Such a study opens up new avenues into the rational design of nanodiagnosis and treatment agents for NIR-II PA imaging and cancer therapy.


Subject(s)
Photoacoustic Techniques , Surface Plasmon Resonance , Tungsten , Animals , Humans , Mice , Tungsten/chemistry , Infrared Rays , Oxides/chemistry , Neoplasms/diagnostic imaging , Neoplasms/therapy , Neoplasms/drug therapy , Nanoparticles/chemistry , Nanoparticles/therapeutic use , Cell Line, Tumor , Reactive Oxygen Species/metabolism
9.
Sensors (Basel) ; 24(9)2024 Apr 27.
Article in English | MEDLINE | ID: mdl-38732912

ABSTRACT

The high affinity of the biotin-streptavidin interaction has made this non-covalent coupling an indispensable strategy for the immobilization and enrichment of biomolecular affinity reagents. However, the irreversible nature of the biotin-streptavidin bond renders surfaces functionalized using this strategy permanently modified and not amenable to regeneration strategies that could increase assay reusability and throughput. To increase the utility of biotinylated targets, we here introduce a method for reversibly immobilizing biotinylated thrombin-binding aptamers onto a Ni-nitrilotriacetic acid (Ni-NTA) sensor chip using 6xHis-tagged streptavidin as a regenerable capture ligand. This approach enabled the reproducible immobilization of aptamers and measurements of aptamer-protein interaction in a surface plasmon resonance assay. The immobilized aptamer surface was stable during five experiments over two days, despite the reversible attachment of 6xHis-streptavidin to the Ni-NTA surface. In addition, we demonstrate the reproducibility of this immobilization method and the affinity assays performed using it. Finally, we verify the specificity of the biotin tag-streptavidin interaction and assess the efficiency of a straightforward method to regenerate and reuse the surface. The method described here will allow researchers to leverage the versatility and stability of the biotin-streptavidin interaction while increasing throughput and improving assay efficiency.


Subject(s)
Aptamers, Nucleotide , Biotin , Nitrilotriacetic Acid , Streptavidin , Surface Plasmon Resonance , Streptavidin/chemistry , Biotin/chemistry , Aptamers, Nucleotide/chemistry , Nitrilotriacetic Acid/chemistry , Nitrilotriacetic Acid/analogs & derivatives , Biosensing Techniques/methods , Thrombin/chemistry , Organometallic Compounds
10.
Sci Rep ; 14(1): 10868, 2024 05 13.
Article in English | MEDLINE | ID: mdl-38740836

ABSTRACT

Therapeutic antibodies have been developed to target amyloid-beta (Aß), and some of these slow the progression of Alzheimer's disease (AD). However, they can also cause adverse events known as amyloid-related imaging abnormalities with edema (ARIA-E). We investigated therapeutic Aß antibody binding to cerebral amyloid angiopathy (CAA) fibrils isolated from human leptomeningeal tissue to study whether this related to the ARIA-E frequencies previously reported by clinical trials. The binding of Aß antibodies to CAA Aß fibrils was evaluated in vitro using immunoprecipitation, surface plasmon resonance, and direct binding assay. Marked differences in Aß antibody binding to CAA fibrils were observed. Solanezumab and crenezumab showed negligible CAA fibril binding and these antibodies have no reported ARIA-E cases. Lecanemab showed a low binding to CAA fibrils, consistent with its relatively low ARIA-E frequency of 12.6%, while aducanumab, bapineuzumab, and gantenerumab all showed higher binding to CAA fibrils and substantially higher ARIA-E frequencies (25-35%). An ARIA-E frequency of 24% was reported for donanemab, and its binding to CAA fibrils correlated with the amount of pyroglutamate-modified Aß present. The findings of this study support the proposal that Aß antibody-CAA interactions may relate to the ARIA-E frequency observed in patients treated with Aß-based immunotherapies.


Subject(s)
Amyloid beta-Peptides , Cerebral Amyloid Angiopathy , Humans , Cerebral Amyloid Angiopathy/immunology , Cerebral Amyloid Angiopathy/pathology , Amyloid beta-Peptides/metabolism , Amyloid beta-Peptides/immunology , Antibodies, Monoclonal, Humanized/therapeutic use , Alzheimer Disease/metabolism , Alzheimer Disease/immunology , Alzheimer Disease/pathology , Protein Binding , Amyloid/metabolism , Amyloid/immunology , Surface Plasmon Resonance
11.
Molecules ; 29(10)2024 May 14.
Article in English | MEDLINE | ID: mdl-38792165

ABSTRACT

The objective of this study was to identify multiple alkaloids in Coptis chinensis that demonstrate inhibitory activity against DPP-4 and systematically evaluate their activity and binding characteristics. A combined strategy that included molecular docking, a DPP-4 inhibition assay, surface plasmon resonance (SPR), and a molecular dynamics simulation technique was employed. The results showed that nine alkaloids in Coptis chinensis directly inhibited DPP-4, with IC50 values of 3.44-53.73 µM. SPR-based binding studies revealed that these alkaloids display rapid binding and dissociation characteristics when interacting with DPP-4, with KD values ranging from 8.11 to 29.97 µM. A molecular dynamics analysis revealed that equilibrium was rapidly reached by nine DPP-4-ligand systems with minimal fluctuations, while binding free energy calculations showed that the ∆Gbind values for the nine test compounds ranged from -31.84 to -16.06 kcal/mol. The most important forces for the binding of these alkaloids with DPP-4 are electrostatic interactions and van der Waals forces. Various important amino acid residues, such as Arg125, His126, Phe357, Arg358, and Tyr547, were involved in the inhibition of DPP-4 by the compounds, revealing a mechanistic basis for the further optimization of these alkaloids as DPP-4 inhibitors. This study confirmed nine alkaloids as direct inhibitors of DPP-4 and characterized their binding features, thereby providing a basis for further research and development on novel DPP-4 inhibitors.


Subject(s)
Alkaloids , Coptis , Dipeptidyl Peptidase 4 , Dipeptidyl-Peptidase IV Inhibitors , Molecular Docking Simulation , Molecular Dynamics Simulation , Dipeptidyl-Peptidase IV Inhibitors/chemistry , Dipeptidyl-Peptidase IV Inhibitors/pharmacology , Coptis/chemistry , Dipeptidyl Peptidase 4/chemistry , Dipeptidyl Peptidase 4/metabolism , Alkaloids/chemistry , Alkaloids/pharmacology , Protein Binding , Humans , Binding Sites , Surface Plasmon Resonance , Drug Discovery/methods
12.
PLoS One ; 19(5): e0304154, 2024.
Article in English | MEDLINE | ID: mdl-38776309

ABSTRACT

Membrane proteins are the main targets of therapeutic drugs and most of them are glycosylated. Glycans play pivotal roles in several biological processes, and glycosylation changes are a well-established hallmark of several types of cancer, including pancreatic cancer, that contribute to tumor growth. Mucin-4 (MUC-4) is a membrane glycoprotein which is associated with pancreatic cancer and metastasis, and it has been targeted as a promising vaccine candidate. In this study, Surface Plasmon Resonance Microscopy (SPRM) was implemented to study complex influences of the native N-glycan cellular environment on binding interactions to the MUC-4 receptor as this is currently the only commercially available label-free technique with high enough sensitivity and resolution to measure binding kinetics and heterogeneity on single cells. Such unique capability enables for a more accurate understanding of the "true" binding interactions on human cancer cells without disrupting the native environment of the target MUC-4 receptor. Removal of N-linked glycans in pancreatic cancer cells using PNGase F exposed heterogeneity in Concanavalin (Con A) binding by revealing three new binding populations with higher affinities than the glycosylated control cells. Anti-MUC-4 binding interactions of enzymatically N-linked deglycosylated pancreatic cancer cells produced a 25x faster association and 37x higher affinity relative to the glycosylated control cells. Lastly, four interaction modes were observed for Helix Pomatia Agglutinin (HPA) binding to the glycosylated control cells, but shifted and increased in activity upon removal of N-linked glycans. These results identified predominant interaction modes of glycan and MUC-4 in pancreatic cancer cells, the kinetics of their binding interactions were quantified, and the influence of N-linked glycans in MUC-4 binding interactions was revealed.


Subject(s)
Mucin-4 , Pancreatic Neoplasms , Polysaccharides , Protein Binding , Surface Plasmon Resonance , Humans , Pancreatic Neoplasms/metabolism , Pancreatic Neoplasms/pathology , Surface Plasmon Resonance/methods , Polysaccharides/metabolism , Mucin-4/metabolism , Cell Line, Tumor , Glycosylation , Microscopy/methods
13.
Bioorg Med Chem Lett ; 107: 129792, 2024 Jul 15.
Article in English | MEDLINE | ID: mdl-38734389

ABSTRACT

Ceramide 1-phosphate (C1P) is a lipid mediator that specifically binds and activates cytosolic phospholipase A2α (cPLA2α). To elucidate the structure-activity relationship of the affinity of C1P for cPLA2α in lipid environments, we prepared a series of C1P analogs containing structural modifications in the hydrophilic parts and subjected them to surface plasmon resonance (SPR). The results suggested the presence of a specific binding site for cPLA2α on the amide, 3-OH and phosphate groups in C1P structure. Especially, dihydro-C1P exhibited enhanced affinity for cPLA2α, suggesting the hydrogen bonding ability of 3-hydroxy group is important for interactions with cPLA2α. This study helps to understand the influence of specific structural moieties of C1P on the interaction with cPLA2α at the atomistic level and may lead to the design of drugs that regulate cPLA2α activation.


Subject(s)
Ceramides , Drug Design , Surface Plasmon Resonance , Ceramides/chemistry , Ceramides/chemical synthesis , Ceramides/metabolism , Structure-Activity Relationship , Group IV Phospholipases A2/metabolism , Group IV Phospholipases A2/antagonists & inhibitors , Humans , Molecular Structure , Binding Sites
14.
Spectrochim Acta A Mol Biomol Spectrosc ; 317: 124417, 2024 Sep 05.
Article in English | MEDLINE | ID: mdl-38728850

ABSTRACT

The use of fluorescent carbon dots (CDs) as highly precise biolabeling probes has been widespread in the fields of live cell imaging and protein labeling due to their small size and excellent photoluminescence ability to accurately target specific molecules with surface chemical properties. However, there was a lack of research on the interaction between CDs and labeled molecules. In this work, we presented a novel investigation strategy, the fluorescence microscopy-surface plasmon resonance (FM-SPR) system, which combined the use of fluorescence microscopy and wavelength modulation surface plasmon resonance to study the interaction between CDs and labeled molecules in real-time. Using this system, simultaneously recorded the SPR signals and the fluorescence images on the surface of the FM-SPR sensor chip. We observed the dynamic curve and fluorescence images of the interaction between green emissive nitrogen-doped carbon dots (N-CDs) and silk fibroin (SF) in real-time. The kinetic parameters, the quantitative analysis, and the investigation of the binding could be achieved. The results showed a strong linear relationship between the change in SPR signals and the concentration of N-CDs, with a linear coefficient of 0.99913. The linear detection range was 2.5 µg/mL-100 µg/mL, and the real lowest detection limit reached 0.5 µg/mL. Additionally, the green fluorescence points in the imaging region on the FM-SPR sensor chip increased with the concentration of N-CDs, which was consistent with the change in SPR signals. Using this system we also acquired the association rate and dissociation rate of N-CDs to SF which were 2.65 × 10-5/s and 1.52 × 10-5/s, respectively. This demonstrated the effectiveness of our method in quantitatively analyzing SF labeled with N-CDs.


Subject(s)
Carbon , Fibroins , Microscopy, Fluorescence , Quantum Dots , Surface Plasmon Resonance , Fibroins/chemistry , Surface Plasmon Resonance/methods , Carbon/chemistry , Quantum Dots/chemistry , Microscopy, Fluorescence/methods , Fluorescent Dyes/chemistry , Animals , Limit of Detection , Kinetics
15.
Zhongguo Zhong Yao Za Zhi ; 49(7): 1848-1864, 2024 Apr.
Article in Chinese | MEDLINE | ID: mdl-38812197

ABSTRACT

Elucidating the quality markers(Q-markers) of traditional Chinese medicines is essential for understanding the mechanisms of action and promoting the rational use of traditional Chinese medicines as well as for developing traditional Chinese medicine-derived drugs. Studies have shown that surface plasmon resonance(SPR) is promising in this field. This study proposed a method based on pull-down with SPR chips to predict the Q-markers of Angong Niuhuang pills(AGNHP). Firstly, 71 main chemical components of AGNHP were analyzed by UPLC-Q-TOF-MS, and then network pharmacology was employed to predict the potential targets of AGNHP against stroke. Secondly, the STAT3 protein chip was constructed, and the extract of AGNHP was recovered by pull-down of the SPR system for STAT3 ligand. The potential active ingredients were collected, enriched, and identified as coptisine, palmatine, epiberberine, berberine, worenine, demethyleneberberine, jatrorrhizine, tetrahydrocoptisine, baicalein, and baicalin methyl ester. Next, the affinity constants of the 10 active ingredients were determined as 44.7, 44, 58.1, 51.3, 39.7, 32.1, 49.2, 69.1, 19.7, and 24.9 µmol·L~(-1), respectively. The molecular docking results showed that the 10 compounds could compete for binding with STAT3. This is the first report that SPR combined with UPLC-Q-TOF-MS is reliable and feasible for determining the active ingredients of AGNHP at the molecular level from complex systems. STAT3 could be used as a potential target for the biological quality evaluation of AGNHP.


Subject(s)
Drugs, Chinese Herbal , Mass Spectrometry , Surface Plasmon Resonance , Drugs, Chinese Herbal/chemistry , Drugs, Chinese Herbal/analysis , Mass Spectrometry/methods , STAT3 Transcription Factor/metabolism , STAT3 Transcription Factor/chemistry , Chromatography, High Pressure Liquid/methods , Chromatography, Liquid/methods , Quality Control , Humans , Liquid Chromatography-Mass Spectrometry
16.
Opt Express ; 32(6): 10077-10092, 2024 Mar 11.
Article in English | MEDLINE | ID: mdl-38571228

ABSTRACT

Every year, millions of people suffer some form of illness associated with the consumption of contaminated food. Escherichia coli (E. coli), found in the intestines of humans and other animals, is commonly associated with various diseases, due to the existence of pathogenic strains. Strict monitoring of food products for human consumption is essential to ensure public health, but traditional cell culture-based methods are associated with long waiting times and high costs. New approaches must be developed to achieve cheap, fast, and on-site monitoring. Thus, in this work, we developed optical fiber sensors based on surface plasmon resonance. Gold and cysteamine-coated fibers were functionalized with anti-E. coli antibody and tested using E. coli suspensions with concentrations ranging from 1 cell/mL to 105 cells/mL. An average logarithmic sensitivity of 0.21 ± 0.01 nm/log(cells/mL) was obtained for three independent assays. An additional assay revealed that including molybdenum disulfide resulted in an increase of approximately 50% in sensitivity. Specificity and selectivity were also evaluated, and the sensors were used to analyze contaminated water samples, which verified their promising applicability in the aquaculture field.


Subject(s)
Biosensing Techniques , Surface Plasmon Resonance , Animals , Humans , Surface Plasmon Resonance/methods , Escherichia coli , Optical Fibers , Biosensing Techniques/methods , Immunoassay
17.
Sensors (Basel) ; 24(7)2024 Mar 26.
Article in English | MEDLINE | ID: mdl-38610339

ABSTRACT

Antibiotic residues have become a worldwide public safety issue. It is vital to detect multiple antibiotics simultaneously using sensors. A new and efficient method is proposed for the combined detection of two antibiotics (enrofloxacin (Enro) and ciprofloxacin (Cip)) in milk using surface plasmon resonance (SPR) sensors. Based on the principle of immunosuppression, two antibiotic antigens (for Enro and Cip) were immobilized on an optical fiber surface with conjugates of bovine serum albumin using dopamine (DA) polymerization. Each single antigen was bound to its corresponding antibody to derive standard curves for Enro and Cip. The fiber-optic sensor's sensitivity was 2900 nm/RIU. Detection limits were calculated to be 1.20 ng/mL for Enro and 0.81 ng/mL for Cip. The actual system's recovery rate was obtained by testing Enro and Cip in milk samples; enrofloxacin's and ciprofloxacin's mean recoveries from the milk samples were 96.46-120.46% and 96.74-126.9%, respectively. In addition, several different regeneration solutions were tested to analyze the two target analytes' regeneration ability; NaOH and Gly-HCl solutions were found to have the best regeneration ability.


Subject(s)
Anti-Bacterial Agents , Surface Plasmon Resonance , Enrofloxacin , Ciprofloxacin , Fiber Optic Technology
18.
Sensors (Basel) ; 24(7)2024 Mar 31.
Article in English | MEDLINE | ID: mdl-38610453

ABSTRACT

Nanozymes possess major advantages in catalysis and biosensing compared with natural nanozymes. In this study, the AuPt@BaTiO3 bimetallic alloy Schottky junction is prepared to act as oxidase mimetics, and its photo-piezoelectric effect is investigated. The synergy between the photo-piezoelectric effect and the local surface plasmon resonance enhances the directional migration and separation of photogenerated electrons, as well as hot electrons induced by the AuPt bimetallic alloy. This synergy significantly improves the oxidase-like activity. A GSH colorimetric detection platform is developed based on this fading principle. Leveraging the photo-piezoelectric effect allows for highly sensitive detection with a low detection limit (0.225 µM) and reduces the detection time from 10 min to 3 min. The high recovery rate (ranging from 99.91% to 101.8%) in actual serum detection suggests promising potential for practical applications. The development of bimetallic alloy heterojunctions presents new opportunities for creating efficient nanozymes.


Subject(s)
Alloys , Colorimetry , Catalysis , Electrons , Surface Plasmon Resonance
19.
ACS Sens ; 9(4): 2110-2121, 2024 Apr 26.
Article in English | MEDLINE | ID: mdl-38622791

ABSTRACT

In this study, we explore the full-spectrum capabilities of fiber-optic surface plasmon resonance (FO-SPR) for analyzing heterogeneous samples with increased comprehensiveness. Our approach involves refining a literature-derived FO-SPR model to more precisely reflect experimental data obtained using a back-reflecting sensor configuration. Key enhancements in our model include adjustments to the thickness and permittivity of the gold SPR-active layer on the FO-SPR sensor as well as improvements to the angular distribution of light within the system. We apply this optimized model to the investigation of the deposition process of a metal-organic framework (MOF), specifically ZIF-8, using FO-SPR. By closely examining the temporal variations in the FO-SPR signal during MOF layer formation, we simultaneously determine the evolving thickness and refractive index (RI) of the MOF layer, offering a dual-parameter analysis. Our results demonstrate that a full-spectrum analysis of the FO-SPR signal can extract critical information from samples exhibiting radial heterogeneity. This advancement significantly enhances the quantitative assessment of various phenomena that alter the refractive index in the sensor's domain, such as adsorption and binding processes. This work thus represents a significant step forward in the field of FO-SPR sensor technology, promising broad applications in areas requiring the precise detection and analysis of complex samples.


Subject(s)
Metal-Organic Frameworks , Surface Plasmon Resonance , Surface Plasmon Resonance/methods , Metal-Organic Frameworks/chemistry , Gold/chemistry , Fiber Optic Technology/methods , Fiber Optic Technology/instrumentation
20.
Appl Opt ; 63(10): 2552-2560, 2024 Apr 01.
Article in English | MEDLINE | ID: mdl-38568535

ABSTRACT

The authors propose a surface plasmon resonance (SPR) sensor based on photonic crystal fibers (PCFs) using three hexagonal ring lattices. The sensor can detect biomolecules with maximum wavelength and amplitude sensitivities of 23,000 nm/RIU and 1310.93R I U -1, respectively, in the RI range of 1.32 to 1.42. It can detect infected red blood cells with Plasmodium falciparum for RIs of 1.402, 1.373, 1.395, and 1.383 in various malaria-infected red blood cell stages, including ring phase, trophozoite phase, and schizont phase. Furthermore, the sensor will be able to detect biomolecules such as viruses, proteins, DNA/RNA strands, acetone, ethanol, hexane, isopropanol, hexanol, formic acid, allyl cyanide, and others in its range. With these impressive results and identification capacity, the proposed sensor would benefit the biomaterial field and be appropriate for the early identification of malaria disease.


Subject(s)
Malaria , Plasmodium falciparum , Humans , Surface Plasmon Resonance , 2-Propanol , Acetone
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