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Adhesion between peptides/antibodies and breast cancer cells
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10.1063/1.3430940
/content/aip/journal/jap/107/11/10.1063/1.3430940
http://aip.metastore.ingenta.com/content/aip/journal/jap/107/11/10.1063/1.3430940

Figures

Image of FIG. 1.
FIG. 1.

Schematic of typical force-displacement plot with corresponding stages of force-displacement behavior (adapted from Ref. 45). In one approach-retract cycle the AFM tip: approaches the surface of the sample (A), jumps to contact with the surface when significant van der Waals forces are felt (B), undergoes elastic bending and is retracted (C) and (D). Due to adhesive interactions, the tip does not detach from the substrate until a force sufficient to pull the tip off of the surface is achieved (E).

Image of FIG. 2.
FIG. 2.

Ligand/receptor interactions. In the experimental setup, ligands on the dip-coated AFM tip sense interactions with the surface receptors on breast cancer cells seeded on a petri dish.

Image of FIG. 3.
FIG. 3.

SEM images of AFM tips such as: (a) bare AFM tip; (b) LHRH-coated AFM tip before adhesion force measurement; (c) LHRH-coated AFM tip after adhesion force measurement; (d) EphA2 Ab-coated AFM tip before adhesion force measurement; (e) EphA2 Ab-coated AFM tip after adhesion force measurement. Boxes indicate coating on tip apex.

Image of FIG. 4.
FIG. 4.

Typical AFM force-displacement behavior for (a) LHRH-coated tip and (b) EphA2 Ab-coated tip on breast cancer cells.

Image of FIG. 5.
FIG. 5.

Summary of pull-off force measurements for (a) LHRH peptide and (b) EphA2 antibody. For (a) LHRH peptide, the average adhesive forces between peptide and receptors on breast cancer cells are nearly five times greater than between peptide and normal breast cells , while values of adhesion force for the controls (bare tip to cancer cells and normal cells) are comparable to each other ( and , respectively). Similarly, for (b) EphA2 Ab, the average adhesive forces between Ab and breast cancer cells are over five times greater than between Ab and normal breast cells , while values for the controls (bare tip to cancer cells and normal cells) are comparable to each other ( and , respectively).

Image of FIG. 6.
FIG. 6.

Confocal microscopy images of LHRH receptor distribution on (a) normal breast cells and (b) breast cancer cells. The images show the overexpression of LHRH receptors (designated by arrows) in the breast cancer cells (b) compared to those on the normal breast cells (a). Nuclei are also identified by arrows.

Image of FIG. 7.
FIG. 7.

Confocal microscopy images of EphA2 receptor distribution on (a) normal breast cells and (b) breast cancer cells. The images show the overexpression of EphA2 receptors (designated by arrows) in the breast cancer cells (b), compared to those on the normal breast cells (a), in which an abundance of EphA2 receptors was found on the cell membrane. Nuclei are also identified by arrows.

Tables

Generic image for table
Table I.

Spring constants of the bare/coated AFM tips.

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Table II.

Adhesion forces between bare/LHRH-coated tips and breast cancer cells/normal breast cells.

Generic image for table
Table III.

Adhesion forces between bare/Ab-coated tips and breast cancer cells/normal breast cells.

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/content/aip/journal/jap/107/11/10.1063/1.3430940
2010-06-01
2014-04-24
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752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
Scitation: Adhesion between peptides/antibodies and breast cancer cells
http://aip.metastore.ingenta.com/content/aip/journal/jap/107/11/10.1063/1.3430940
10.1063/1.3430940
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