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Porous Peptide Complexes by a Folding-and-Assembly Strategy
Tomohisa Sawada1, Motoya Yamagami1, Shuji Akinaga1
1Department of Applied Chemistry, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8656, Japan.
Chemistry, an Asian Journal
|April 6, 2017
Summary
Synthetic chemists created a novel porous peptide structure using a coordination-driven folding and assembly strategy. This method yielded a framework with large pores and a stable helical conformation, enabling further modifications.
Area of Science:
- Supramolecular chemistry
- Materials science
- Peptide chemistry
Background:
- Protein self-assembly relies on coordinated folding and assembly, a strategy seldom mimicked by synthetic chemists.
- Developing synthetic analogues for complex biological structures remains a challenge.
Purpose of the Study:
- To design and synthesize a novel porous peptide structure using a coordination-driven folding-and-assembly approach.
- To investigate the formation of a PII helical peptide scaffold within a porous framework.
Main Methods:
- Utilized a coordination-driven strategy involving AgNTf2 and tripeptide ligands with a Gly-Pro-Pro sequence.
- Employed complexation to achieve folding and assembly of peptide ligands into a porous framework.
- Investigated post-synthetic modification of the porous structure while maintaining the peptide conformation.
Main Results:
- Successfully synthesized a porous framework with 1.5 nm-sized pores.
- Obtained a stable PII helical peptide scaffold within the porous structure.
- Demonstrated the ability to modify the pore environment without disrupting the helical conformation.
Conclusions:
- The coordination-driven folding-and-assembly strategy is effective for creating complex porous peptide materials.
- The resulting PII helical peptide scaffold is robust and amenable to further functionalization.
- This work provides a new platform for designing advanced peptide-based porous materials.