Molography for integrin-mediated cancer cell adhesion

About the talk

Recorded at the 3rd focal Molography User Meeting on September 9, 2026. Szabolcs Novák (HUN-REN Centre for Energy Research) shows how focal molography follows the adhesion of living cancer cells to RGD-functionalized sensor chips and separates where integrins bind from how much mass arrives at the surface.

Topics covered

• From molecules to living cells. Integrins link the cell to its surroundings, recognize the RGD peptide motif and are overexpressed in many tumors. The Nanobiosensorics Laboratory has studied their adhesion kinetics with label-free biosensors, single-cell force methods and holographic microscopy, but evanescent-field sensors cannot tell specific integrin binding from nonspecific mass.
• An open-channel cell protocol. HeLa cells are pipetted onto click chemistry chips that carry RGD on the mologram ridges and a protein-repellent PEG layer in the grooves, then imaged by microscopy. Vinculin staining confirms that the cells adhere through integrins on the molograms.
• Three phases of adhesion. In the first phase, coherent and total mass rise together as nascent adhesions form on the ridges. In the second phase, the coherent signal falls while mass keeps arriving, because focal adhesions grow out into the grooves. In the third phase, the coherent signal recovers as adhesions mature back along the ridges.
• Integrin numbers per cell. With an analyte efficiency of about 10%, the integrin count per HeLa cell lands in the same order of magnitude as earlier estimates from other biosensors, which supports this value as a working approximation.
• Cells respond to treatment. EDTA releases the cells, neuraminidase removes sialic acid from the glycocalyx and gives a weaker, slower coherent signal, and histamine changes adhesion in line with earlier measurements. A first experiment on DNA chips with cyclic RGD points to reusable surfaces.