7TM1

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

7TM1 の概要

• エントリーDOI: 10.2210/pdb7tm1/pdb
• 分子名称: bipyridyl-conjugated helical peptide, ACETONITRILE (3 entities in total)
• 機能のキーワード: porous, framework, helix, 310, alpha, assembly, bipyridine, uic-1, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 4345.17

構造登録者

Nguyen, A.I. (登録日: 2022-01-19, 公開日: 2022-04-20, 最終更新日: 2024-09-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.1 Å)