A New Building Block for Nanostructures
NMR, crystallography, and native MS reveal a modular protein–foldamer interface for assembling defined molecular architectures
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NMR, crystallography, and native MS reveal a modular protein–foldamer interface for assembling defined molecular architectures
Researchers developed a modular protein–foldamer pair for assembling hybrid nanostructures with controlled geometry.
The protein–foldamer interface offers a large, well-defined binding surface, improving assembly positioning compared to existing methods.
C10, a variant of the Nanofitin scaffold, was identified as a selective protein partner for the helical aromatic foldamer.
Binding studies revealed that C10 binds the foldamer with nanomolar affinity, enabling stable architectural designs.
The study demonstrates that artificial foldamers can serve as precise connectors for protein architectures, allowing for customizable assembly.
This content is an AI-generated, fully rewritten summary based on a published scholarly article. It does not reproduce the original text and is not a substitute for the original publication. Readers are encouraged to consult the source for full context, data, and methodology.
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