7TME

Porous framework formed by assembly of a bipyridyl-conjugated helical peptide

Summary for 7TME

• Entry DOI: 10.2210/pdb7tme/pdb
• Descriptor: bipyridyl-conjugated helical peptide, ACETONITRILE (3 entities in total)
• Functional Keywords: porous, framework, helix, 310, alpha, assembly, bipyridine, uic-1, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 1486.68

Authors

Nguyen, A.I. (deposition date: 2022-01-19, release date: 2023-01-25, Last modification date: 2024-09-25)

Primary citation

Heinz-Kunert, S.L.,Pandya, A.,Dang, V.T.,Tran, P.N.,Ghosh, S.,McElheny, D.,Santarsiero, B.D.,Ren, Z.,Nguyen, A.I.
Assembly of pi-Stacking Helical Peptides into a Porous and Multivariable Proteomimetic Framework.
J.Am.Chem.Soc., 144:7001-7009, 2022

PubMed Abstract: The evolution of proteins from simpler, self-assembled peptides provides a powerful blueprint for the design of complex synthetic materials. Previously, peptide-metal frameworks using short sequences (≤3 residues) have shown great promise as proteomimetic materials that exhibit sophisticated capabilities. However, their development has been hindered due to few variable residues and restricted choice of side-chains that are compatible with metal ions. Herein, we developed a noncovalent strategy featuring π-stacking bipyridyl residues to assemble much longer peptides into crystalline frameworks that tolerate even previously incompatible acidic and basic functionalities and allow an unprecedented level of pore variations. Single-crystal X-ray structures are provided for all variants to guide and validate rational design. These materials exhibit hallmark proteomimetic behaviors such as guest-selective induced fit and assembly of multimetallic units. Significantly, we demonstrate facile optimization of the framework design to substantially increase affinity toward a complex organic molecule.

PubMed: 35390261
DOI: 10.1021/jacs.2c02146

Experimental method

X-RAY DIFFRACTION (0.8 Å)