Real-time analysis of the carbohydrates on cell surfaces using a QCM biosensor: a lectin-based approach

Pei, Zhichao; Saint-Guirons, Julien; Käck, Camilla; Ingemarsson, Björn; Aastrup, Teodor

doi:10.1016/j.bios.2012.02.047

Cited by 50 publications

(39 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The applicability of the QCM technology for monitoring real‐time binding of lectins with carbohydrates or glycoproteins has previously been evaluated with immobilized lectins ,, and carbohydrates . Indeed, lectin‐cell interaction has been evaluated with immobilized lectins or cells on chip surface and opens a new possibility of characterization of tumor cells glycan. In this study, the affinity of interaction between leukemia cells, on flux, and the lectin, immobilized on QCM biosensor chip surface, was assessed in order to better understand the correlation between lectin‐cell binding and cytotoxicity process.…”

Section: Resultsmentioning

confidence: 99%

ArtinM Binding Effinities and Kinetic Interaction with Leukemia Cells: A Quartz Crystal Microbalance Bioelectroanalysis on the Cytotoxic Effect

et al. 2017

View full text Add to dashboard Cite

ArtinM, a D‐mannose‐binding lectin from Artocarpus heterophyllus (jackfruit), interacts with N‐glycosylated receptors on the surface of several cells of hematopoietic origin, triggering cell migration, degranulation, and cytokine release. Because malignant transformation is often associated with altered expression of cell surface glycans, we evaluated the interaction of ArtinM with human myelocytic leukemia cells by Quartz Cristal Microbalance (QCM) and cross compared this investigation with cellular responses (cytotoxicity) to lectin binding by the colorimetric assay MTT, which is a standard method in biology. QCM analysis was able to provide additional information (not possible to be obtained by MTT) that impact on the knowledge of medical biology related to leukemic cells. For instance, it was shown that association rate constant of ArtinM and cellular membranes (obtained from QCM) of leukemia cell varies across the myeloid leukemia cell lines, decreasing as cytotoxic effect increases. Meanwhile no differences were observed for dissociation rate constants so that the equilibrium binding affinity constant was observed to be a direct function of the association rate event. It was supposed that ArtinM cytotoxicity is affected by the association time with glycans on the cellular membranes of leukemia cells in a way that the higher it is the association time (the lower was the association rate constant) the higher is the ArtinM cytotoxicity over the leukemia cell lines.

show abstract

Section: Resultsmentioning

confidence: 99%

ArtinM Binding Effinities and Kinetic Interaction with Leukemia Cells: A Quartz Crystal Microbalance Bioelectroanalysis on the Cytotoxic Effect

et al. 2017

View full text Add to dashboard Cite

show abstract

“…, ArtinM lectin) can be readily obtained by using the Langmuir adsorption isotherm model [ 16 , 29 ]. The 1:1 interaction model was used as previously described [ 16 , 32 ], even with multiple sites of interaction on cells, and more than one site of interaction on ArtinM. Consequently,

represents herein an average of lectin–multiple sites interaction.…”

Section: Resultsmentioning

confidence: 99%

“…In summary, the results clearly demonstrate that affinity estimated through

differs depending on whether EIS or QCM analysis is used for a lectin–cell binding model under Langmuir model premises. The capability of evaluating

as demonstrated herein can be helpful in tumor cell characterization and in the study of drug delivery [ 32 , 33 , 34 , 38 ].…”

Section: Resultsmentioning

confidence: 99%

“…QCM and EIS techniques have also been used to characterize lectin–cell interactions, including cell-surface glycosylation [ 32 , 33 ] or discrimination among malignant stages of tumor cells [ 19 , 32 , 33 , 34 ]. In this study, we performed the first comparative evaluation of the sensitivity between piezoelectric (by QCM) and impedimetric (by EIS) approaches in determining lectin–cell interactions.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Evaluating the Equilibrium Association Constant between ArtinM Lectin and Myeloid Leukemia Cells by Impedimetric and Piezoelectric Label Free Approaches

et al. 2014

View full text Add to dashboard Cite

Label-free methods for evaluating lectin–cell binding have been developed to determine the lectin–carbohydrate interactions in the context of cell-surface oligosaccharides. In the present study, mass loading and electrochemical transducer signals were compared to characterize the interaction between lectin and cellular membranes by measuring the equilibrium association constant, Ka, between ArtinM lectin and the carbohydrate sites of NB4 leukemia cells. By functionalizing sensor interfaces with ArtinM, it was possible to determine Ka over a range of leukemia cell concentrations to construct analytical curves from impedimetric and/or mass-associated frequency shifts with analytical signals following a Langmuir pattern. Using the Langmuir isotherm-binding model, the Ka obtained were (8.9 ± 1.0) × 10−5 mL/cell and (1.05 ± 0.09) × 10−6 mL/cell with the electrochemical impedance spectroscopy (EIS) and quartz crystal microbalance (QCM) methods, respectively. The observed differences were attributed to the intrinsic characteristic sensitivity of each method in following Langmuir isotherm premises.

show abstract

“…Furthermore, QCM sensor was useful for evaluating changes of carbohydrate chains of cancer cells associated with tumor growth and metastasis. In fact, Pei and coworkers immobilized an epidermoid carcinoma cell line (A-4531) and a breast adenocarcinoma cell line (MDA-MB-468) on quartz crystals to evaluate the binding of lectins [120]. The gravimetric response of the QCM sensors was sensitive to the glycosylation changes of the cells associated with cancer progression and development.…”

Section: Cytosensorsmentioning

confidence: 99%

Recent Progress in Lectin-Based Biosensors

Wang

Anzai

2015

Materials

View full text Add to dashboard Cite

This article reviews recent progress in the development of lectin-based biosensors used for the determination of glucose, pathogenic bacteria and toxins, cancer cells, and lectins. Lectin proteins have been widely used for the construction of optical and electrochemical biosensors by exploiting the specific binding affinity to carbohydrates. Among lectin proteins, concanavalin A (Con A) is most frequently used for this purpose as glucose- and mannose-selective lectin. Con A is useful for immobilizing enzymes including glucose oxidase (GOx) and horseradish peroxidase (HRP) on the surface of a solid support to construct glucose and hydrogen peroxide sensors, because these enzymes are covered with intrinsic hydrocarbon chains. Con A-modified electrodes can be used as biosensors sensitive to glucose, cancer cells, and pathogenic bacteria covered with hydrocarbon chains. The target substrates are selectively adsorbed to the surface of Con A-modified electrodes through strong affinity of Con A to hydrocarbon chains. A recent topic in the development of lectin-based biosensors is a successful use of nanomaterials, such as metal nanoparticles and carbon nanotubes, for amplifying output signals of the sensors. In addition, lectin-based biosensors are useful for studying glycan expression on living cells.

show abstract

Real-time analysis of the carbohydrates on cell surfaces using a QCM biosensor: a lectin-based approach

Cited by 50 publications

References 24 publications

ArtinM Binding Effinities and Kinetic Interaction with Leukemia Cells: A Quartz Crystal Microbalance Bioelectroanalysis on the Cytotoxic Effect

ArtinM Binding Effinities and Kinetic Interaction with Leukemia Cells: A Quartz Crystal Microbalance Bioelectroanalysis on the Cytotoxic Effect

Evaluating the Equilibrium Association Constant between ArtinM Lectin and Myeloid Leukemia Cells by Impedimetric and Piezoelectric Label Free Approaches

Recent Progress in Lectin-Based Biosensors

Contact Info

Product

Resources

About