Reaction pathway and free energy profile determined for specific recognition of oligosaccharide moiety of carboxypeptidase Y

Senkara-Barwijuk, Elżbieta; Kobiela, Tomasz; Lebed, K.; Lekka, Małgorzata

doi:10.1016/j.bios.2012.04.014

Cited by 18 publications

(17 citation statements)

References 38 publications

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“…The binding kinetics of lectin-carbohydrate interactions is gaining attention due to the fact that cancer cells change their glycosylation profile as they advance, which could be a potential therapeutic target [74].…”

Section: Leukemia Cell Linementioning

confidence: 99%

Application of Biosensors in Cancers, An Overview

Quazi¹

2022

Preprint

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The deadliest disease in the world, cancer, kills many people every year. The early detection is the only hope for the survival of malignant cancer patients. As a result, in the preliminary stages of , the diagnosis of cancer biomarkers at the cellular level is critical for improving cancer patient survival rates. For decades, scientists have focused their efforts on the invention of biosensors. Biosensors, in addition to being employed in other practical scenarios, can essentially function as cost effective and highly efficient devices for this purpose. Traditional cancer screening procedures are expensive, time-consuming, and inconvenient for repeat screenings. Biomarker-based cancer diagnosis, on the other hand, is rising as one of the most potential tools for early detection, disease progression monitoring, and eventual cancer treatment. As Biosensor is an analytical device, it allows the selected analyte to bind to the biomolecules being studied (– for example RNA, DNA, tissue, proteins, cells). They can be divided based on the kind of biorecognition or transducer elements on the sensor. Most biosensor analyses necessitate the analyte being labeled with a specific marker. In this review article, the application of distinct variants of biosensors against cancer has been described.

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Section: Leukemia Cell Linementioning

confidence: 99%

Application of Biosensors in Cancers, An Overview

Quazi¹

2022

Preprint

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“…Apart from the imaging aspect, AFM can also be applied to probe molecular interactions with a force resolution of tenths of pN. This method enables the measurement of the strength of the interaction forces between a single pair of molecules [5][6][7] such as biotin-avidin, biotin-streptavidin [8], or lectin-carbohydrate [9]. Direct measurements of intermolecular forces for complementary DNA strands have been carried out as well [10].…”

Section: Introductionmentioning

confidence: 99%

“…Therefore, studies of the interaction forces provide valuable insight into the mechanisms behind biological interactions. AFM allows for a unique opportunity to probe the properties of individual ligand-receptor complexes and provides details on the structure and behavior of single molecules in conditions close to natural ones [6][7][8][9]. This technique provides several advantages over traditional methods including, for example, characterization of states that are undetectable in ensemble approaches where the average value of a property is monitored.…”

Section: Introductionmentioning

confidence: 99%

Probing fibronectin–antibody interactions using AFM force spectroscopy and lateral force microscopy

Kulik¹,

Lekka²,

Lee³

et al. 2016

Nano Online

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“…Apart from the imaging aspect, AFM can also be applied to probe molecular interactions with a force resolution of tenths of pN. This method enables the measurement of the strength of the interaction forces between a single pair of molecules [ 5 – 7 ] such as biotin–avidin, biotin–streptavidin [ 8 ], or lectin–carbohydrate [ 9 ]. Direct measurements of intermolecular forces for complementary DNA strands have been carried out as well [ 10 ].…”

Section: Introductionmentioning

confidence: 99%

“…Therefore, studies of the interaction forces provide valuable insight into the mechanisms behind biological interactions. AFM allows for a unique opportunity to probe the properties of individual ligand–receptor complexes and provides details on the structure and behavior of single molecules in conditions close to natural ones [ 6 – 9 ]. This technique provides several advantages over traditional methods including, for example, characterization of states that are undetectable in ensemble approaches where the average value of a property is monitored.…”

Section: Introductionmentioning

confidence: 99%

Probing fibronectin–antibody interactions using AFM force spectroscopy and lateral force microscopy

Kulik¹,

Lekka²,

Lee³

et al. 2015

Beilstein J. Nanotechnol.

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SummaryThe first experiment showing the effects of specific interaction forces using lateral force microscopy (LFM) was demonstrated for lectin–carbohydrate interactions some years ago. Such measurements are possible under the assumption that specific forces strongly dominate over the non-specific ones. However, obtaining quantitative results requires the complex and tedious calibration of a torsional force. Here, a new and relatively simple method for the calibration of the torsional force is presented. The proposed calibration method is validated through the measurement of the interaction forces between human fibronectin and its monoclonal antibody. The results obtained using LFM and AFM-based classical force spectroscopies showed similar unbinding forces recorded at similar loading rates. Our studies verify that the proposed lateral force calibration method can be applied to study single molecule interactions.

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Reaction pathway and free energy profile determined for specific recognition of oligosaccharide moiety of carboxypeptidase Y

Cited by 18 publications

References 38 publications

Application of Biosensors in Cancers, An Overview

Application of Biosensors in Cancers, An Overview

Probing fibronectin–antibody interactions using AFM force spectroscopy and lateral force microscopy

Probing fibronectin–antibody interactions using AFM force spectroscopy and lateral force microscopy

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