To develop a modular protein–foldamer pair for assembling hybrid nanostructures with controlled geometry.
Approach:
Development of Protein-Foldamer Pair: Researchers at Ludwig-Maximilians-Universität München created a protein–foldamer pair designed to act as a modular molecular connector, using ribosome display to identify a suitable protein partner.
Binding Affinity Assessment: Biolayer interferometry was employed to demonstrate that the identified protein variant C10 binds the foldamer with nanomolar affinity.
Structural Analysis: Nuclear magnetic resonance spectroscopy and X-ray crystallography were used to elucidate the binding interactions between the foldamer and the C10 scaffold.
Assembly Characterization: Mass spectrometry and ion mobility measurements were utilized to analyze larger assemblies formed from the foldamer and protein components.
Key Findings:
The C10 protein variant binds selectively to the right-handed P-helix of the foldamer with high affinity.
The binding interface features a large contact surface with stable interactions, enabling modular assembly.
The researchers demonstrated the ability to vary the spacing and orientation of proteins by altering foldamer length and geometry.
The resulting structures included cyclic assemblies and a one-dimensional zigzag network with porous characteristics.
Limitations:
The work represents a proof-of-principle rather than a fully developed material.
Further research is needed to explore the practical applications of these structures.
