8ddg | pdb_00008ddg
FYF peptide forms a standard beta-sheet
Structural highlights
Publication Abstract from PubMedThe rippled beta-sheet is a peptidic structural motif related to but distinct from the pleated beta-sheet. Both motifs were predicted in the 1950s by Pauling and Corey. The pleated beta-sheet was since observed in countless proteins and peptides and is considered common textbook knowledge. Conversely, the rippled beta-sheet only gained a meaningful experimental foundation in the past decade, and the first crystal structural study of rippled beta-sheets was published as recently as this year. Noteworthy, the crystallized assembly stopped at the rippled beta-dimer stage. It did not form the extended, periodic rippled beta-sheet layer topography hypothesized by Pauling and Corey, thus calling the validity of their prediction into question. NMR work conducted since moreover shows that certain model peptides rather form pleated and not rippled beta-sheets in solution. To determine whether the periodic rippled beta-sheet layer configuration is viable, the field urgently needs crystal structures. Here we report on crystal structures of two racemic and one quasi-racemic aggregating peptide systems, all of which yield periodic rippled antiparallel beta-sheet layers that are in excellent agreement with the predictions by Pauling and Corey. Our study establishes the rippled beta-sheet layer configuration as a motif with general features and opens the road to structure-based design of unique supramolecular architectures. The rippled beta-sheet layer configuration-a novel supramolecular architecture based on predictions by Pauling and Corey.,Hazari A, Sawaya MR, Vlahakis N, Johnstone TC, Boyer D, Rodriguez J, Eisenberg D, Raskatov JA Chem Sci. 2022 Jul 15;13(31):8947-8952. doi: 10.1039/d2sc02531k. eCollection 2022 , Aug 10. PMID:36091211[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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