Observing dynamic conformational changes of laminin isoforms using high-speed atomic force microscopy

Lucky Akter, Holger Flechsig, Arin Marchesi, and Clemens M. Franz

Int. J. Mol. Sci. 2024

The dancing full-length laminin in higher resolution

While advanced microscopy techniques have previously facilitated the imaging of cross-shaped laminin proteins, these methods were limited to capturing snapshots of individual conformational states or producing low-resolution dynamic images lacking submolecular details.

This study reported an optimized method for studying the dynamic motion of full-length laminin protein under physiological conditions using high-speed atomic force microscopy.

The cell adhesion domain of the examined Biolaminin protein isoforms displayed structural dynamism, alternating between open and compact conformations. This suggests that the cell-binding interface could be more dynamic than previously thought, potentially influencing adhesion receptor binding.

Full-length laminin as the innate cell culture matrix

As a multi-adapter protein, laminin functions as a bridge connecting cells to the extracellular matrix network, transiting signals into the cell.

Laminin is not a static molecule but moves dynamically along the entire full-length configuration, influencing cell survival and identity.

Dynamic movements of full-length laminin protein were observed using high-speed atomic force microscopy. (Akter et al. 2024, video S4, CC BY 4.0)

Unlike fragmented products, the only full-length laminin product, Biolaminin®, provides cells with comprehensive in vivo signaling in vitro.