8gl4
From Proteopedia
Porous framework formed by assembly of a bipyridyl-conjugated helical peptide
Structural highlights
Publication Abstract from PubMedThough thiols are exceptionally versatile, their high reactivity has also hindered the synthesis and characterization of well-defined thiol-containing porous materials. Leveraging the mild conditions of the noncovalent peptide assembly, we readily synthesized and characterized a number of frameworks with thiols displayed at many unique positions and in several permutations. Importantly, nearly all assemblies were structurally determined using single-crystal X-ray diffraction to reveal their rich sequence-structure landscape and the cooperative noncovalent interactions underlying their assembly. These observations and supporting molecular dynamics calculations enabled rational engineering by the positive and negative design of noncovalent interactions. Furthermore, the thiol-containing frameworks undergo diverse single-crystal-to-single-crystal reactions, including toxic metal ion coordination (e.g., Cd(2+), Pb(2+), and Hg(2+)), selective uptake of Hg(2+) ions, and redox transformations. Notably, we find a framework that supports thiol-nitrosothiol interconversion, which is applicable for biocompatible nitric oxide delivery. The modularity, ease of synthesis, functionality, and well-defined nature of these peptide-based thiol frameworks are expected to accelerate the design of complex materials with reactive active sites. Noncovalent Peptide Assembly Enables Crystalline, Permutable, and Reactive Thiol Frameworks.,Hess SS, Coppola F, Dang VT, Tran PN, Mickel PJ, Oktawiec J, Ren Z, Kral P, Nguyen AI J Am Chem Soc. 2023 Sep 13;145(36):19588-19600. doi: 10.1021/jacs.3c03645. Epub , 2023 Aug 28. PMID:37639365[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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