The target affinity and selectivity of many biomacromolecules depend on the three-dimensional (3D) distribution of multiple ligands on their surfaces. Here, we devised a self-assembly strategy to control the target-tailored 3D distribution of multiple α-helical ligands on a coiled-coil core scaffold using novel lariat-type supramolecular building blocks. Depending on the coiled-coil composition and ligand grafting sites in the lariat building blocks, the structural and functional features of the self-assembled peptide nanostructures (SPNs) could be variably fine-tuned. Using oligovalent protein-RNA (Rev-RRE) interactions as a model system, we demonstrate that longer grafting reinforces the helicity of the peptide ligands, whereas shorter grafting strengthens the target binding affinity of the SPNs in both monovalent and oligovalent interactions. This supramolecular approach should be useful in developing precisely controllable multivalent ligands for biomacromolecular interactions.
Bibliographical noteFunding Information:
We thank the Pohang Accelerator Laboratory (PAL) and the Mokpo National University Central Laboratory (MNUCL) for use of the SAXS facility and AUC, respectively. This work was supported by grants from the National Research Foundation ( N R F ) o f Ko r e a ( 2 0 1 4 R 1 A 2A1 A 1 1 0 5 0 3 5 9 , 2014M3A7B4051594) and the Yonsei University Futureleading Research Initiative.
© 2016 American Chemical Society.
All Science Journal Classification (ASJC) codes
- Organic Chemistry
- Polymers and Plastics
- Inorganic Chemistry
- Materials Chemistry