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- W4376644008 abstract "De novo design of peptide nanoshapes is of great interest in biomolecular science since the local peptide nanoshapes formed by a short peptide chain in the proteins are often key to the biological activities. Here, we show that the de novo design of peptide nanoshapes with sub-nanometer conformational control can be realized using peptides consisting of N-methyl-L-alanine and N-methyl-D-alanine residues as studied by NMR, X-ray and XFEL crystallographic and computational analyses as well as by direct imaging of the dynamics of the peptide’s nanoshape using cinematographic electron microscopic technique. The conformation of N-methyl-L/D-alanine residue is largely fixed because of the restricted bond rotation, and hence can serve as a scaffold on which we can build a peptide into a designed nanoshape. The local shape control by per-residue conformational restriction by torsional strains starkly contrasts with the global shape stabilization of proteins based on many remote interactions. The oligomers allow the bottom-up design of diverse peptide nanoshapes with a small number of amino acid residues and would offer unique opportunities to realize the de novo design of biofunctional molecules, such as catalysts and drugs." @default.
- W4376644008 created "2023-05-17" @default.
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- W4376644008 date "2023-05-16" @default.
- W4376644008 modified "2023-10-17" @default.
- W4376644008 title "Bottom-up design of peptide nanoshapes in water using oligomers of N-methyl-L/D-alanine" @default.
- W4376644008 doi "https://doi.org/10.26434/chemrxiv-2023-c4mw6" @default.
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