Assembly of π-Stacking Helical Peptides into a Porous and Multivariable Proteomimetic Framework

Area of Science:

• Supramolecular Chemistry
• Materials Science
• Biomimetic Design

Background:

• Protein evolution from peptides offers a model for synthetic material design.
• Existing peptide-metal frameworks (≤3 residues) are limited by short sequences and incompatible side chains.
• These limitations hinder the development of versatile proteomimetic materials.

Purpose of the Study:

• To develop a novel noncovalent strategy for assembling longer peptides into crystalline frameworks.
• To overcome limitations of short peptide sequences and expand compatible functionalities.
• To create tunable porous materials with enhanced proteomimetic capabilities.

Main Methods:

• Utilized a noncovalent strategy with π-stacking bipyridyl residues.
• Assembled longer peptide sequences into crystalline frameworks.
• Employed single-crystal X-ray crystallography for structural validation.

Main Results:

• Developed crystalline frameworks from longer peptides tolerating diverse functionalities.
• Achieved unprecedented control over pore variations within the frameworks.
• Demonstrated proteomimetic behaviors including guest-selective induced fit and multimetallic assembly.
• Showcased facile optimization for increased affinity toward complex organic molecules.

Conclusions:

• The developed strategy enables the design of advanced, tunable peptide-metal frameworks.
• These materials exhibit sophisticated proteomimetic functions and potential for molecular recognition.
• The findings pave the way for next-generation synthetic materials inspired by protein evolution.