Structural highlights
Publication Abstract from PubMedThe 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 pi-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. Assembly of pi-Stacking Helical Peptides into a Porous and Multivariable Proteomimetic Framework.,Heinz-Kunert SL, Pandya A, Dang VT, Tran PN, Ghosh S, McElheny D, Santarsiero BD, Ren Z, Nguyen AI J Am Chem Soc. 2022 Apr 20;144(15):7001-7009. doi: 10.1021/jacs.2c02146. Epub, 2022 Apr 7. PMID:35390261[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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