A new class of protein material that interacts with living cells without being absorbed by them can influence cell signaling, a new study shows. The material does this by binding and sequestering cell surface receptors. The discovery could have far-reaching implications for stem cell research and enable the development of new materials designed to modulate the behavior of living systems.
The discovery could have far-reaching implications for stem cell research and enable the development of new materials designed to modulate the behavior of living systems.
The research, reported in the January 6 edition of Nature, was led by the Baker lab at the University of Washington School of Medicine and the Derivery lab at the Medical Research Council Laboratory of Molecular Biology in Cambridge, U.K. Their paper is titled, Design of Biologically Active Binary Protein 2D Materials.
Cells interact with their environment via receptors at their surface. These receptors can bind to hormones, neurotransmitters, drugs, and toxins. When such molecules bind to a receptor, this triggers a response inside the cell, a process known as signaling.
But for the cell, it is important that this response be transient, to still be responsive to the signal later on. To achieve this, cells will commonly terminate signaling by absorbing both an activated receptor and the molecule that stimulated it, thereby targeting both for destruction inside the cell.
«This tendency of cells to internalize receptors likely lowers the efficiency of immunotherapies,» said Emmanuel Derivery, assistant professor at the MRC Laboratory of Molecular Biology. «Indeed, when antibody drugs bind their target receptors and then become internalized and degraded, more antibody must always be injected.»
To create a way around this, Baker lab postdoctoral scholar Ariel Ben-Sasson designed new proteins that assemble into large, flat patches. This molecular scaffolding was then further engineered to contain signaling molecules.
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Materials provided by University of Washington Health Sciences/UW Medicine. Original written by Ian Haydon. Note: Content may be edited for style and length.