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Updated: May 24, 2026
Micropatterned Surfaces to Study Hyaluronic Acid Interactions with Cancer Cells
Published on: December 22, 2010
A novel approach to determining the affinity of protein-carbohydrate interactions employing adherent cancer cells
Diluka Peiris1, Anatoliy Markiv1, G Paul Curley1
1Department of Molecular and Applied Biosciences, School of Life Sciences, University of Westminster, 115 New Cavendish St., London W1W 6UW, England, UK.
Abstract:
The development of biological agents for the treatment of solid tumours is an area of considerable activity. We are pursuing carbohydrate-binding proteins (lectins) in a strategy aimed at targeting cancer-associated changes in glycosylation. To evaluate lectin-cancer cell interactions we developed a novel cell biosensor in which binding events take place at the cell surface, more closely mimicking an in vivo system. Metastatic, SW620, and non-metastatic, SW480, colorectal cancer cells were grown on the surface of a tissue-culture compatible polystyrene coated biosensor chip and housed in a quartz crystal microbalance (QCM) apparatus, the kinetics of binding of a diverse range of lectins was evaluated. The lectin Helix pomatia agglutinin (HPA) has been shown to bind aggressive metastatic cancer and was produced in recombinant form (His- and RFP-tagged). The affinity of HPA was in the nanomolar range to the metastatic SW620 cells but was only in the micromolar range to the non-metastatic SW480. Overall, the dissociation constant (K(D)) of the lectins tested in the new cell biosensor system was an order of magnitude lower (nanomolar range) than has generally been reported with systems such as QCM/SPR. This new cell-biosensor enables molecular interactions to be studied in a more relevant environment. An intrinsic problem with developing new biological therapies is the difficulty in determining the affinity with which proteins will interact with intact cell surfaces. This methodology will be of interest to researchers developing new biological approaches for targeting cell surfaces in a wide range of diseases, including cancer.
Insights
Researchers developed a novel cell biosensor to study lectin-cancer cell interactions. This system accurately measures lectin binding affinity to cancer cells, aiding the development of targeted cancer therapies.
Area of Science:
- Biotechnology
- Cancer Research
- Molecular Biology
Background:
- Biological agents for solid tumor treatment are under active development.
- Targeting cancer-associated glycosylation changes is a key strategy.
- Evaluating lectin-cancer cell interactions requires precise methodologies.
Purpose of the Study:
- To develop and validate a novel cell biosensor for studying lectin-cancer cell interactions.
- To mimic in vivo conditions by enabling binding events at the cell surface.
- To assess the binding kinetics and affinity of various lectins to different cancer cell types.
Main Methods:
- A novel cell biosensor was developed using a quartz crystal microbalance (QCM) apparatus.
- Metastatic (SW620) and non-metastatic (SW480) colorectal cancer cells were cultured on a biosensor chip.
- The binding kinetics of diverse lectins, including recombinant Helix pomatia agglutinin (HPA), were evaluated.
Main Results:
- The cell biosensor system demonstrated high sensitivity, with lectin dissociation constants (K(D)) in the nanomolar range.
- Recombinant HPA showed nanomolar affinity for metastatic SW620 cells, but only micromolar affinity for non-metastatic SW480 cells.
- The biosensor provided an order of magnitude lower K(D) values compared to traditional QCM/SPR systems.
Conclusions:
- The novel cell biosensor provides a more relevant environment for studying molecular interactions at the cell surface.
- This methodology overcomes challenges in determining protein-cell surface binding affinity for intact cells.
- The biosensor is valuable for researchers developing cell surface-targeting biological therapies for various diseases, including cancer.
