Enzyme-Mimicking Active Site Clefts Demonstrated by Self-Assembled Peptide Nanoribbons with Polar Zippers.

Due to the inherent limitations of natural enzymes, biomimetic enzymes have received tremendous attention, among which those arising from peptide self-assembly are of particular interest due to their resemblance to natural enzymes in composition and hierarchical structures, as well as their structural robustness and designability. Despite considerable advances achieved in this area, it remains a major challenge to construct active site clefts through peptide self-assembly. Here, we report the design of polar zippers between peptide β-sheets to mimic the catalytic microenvironment of natural enzymes.

Chirality Inversion upon Coassembly of Stereoisomeric Short Peptides with Like-Handedness.

Despite numerous reports devoted to chirality inversion during the self-assembly of single chiral components, chirality inversion in the coassembly of two or more chiral components remains largely unexplored. Here we report the supramolecular chirality inversion via the coassembly of the two different stereoisomers of a minimalistic amphiphilic IK sequence with like-handedness in their self-sorting assembly. The coassembled nanofibrils exhibit noticeable helix inversion in a wide range of mixing ratios, compared to individual peptide nanofibrils.

Peptide Self-Assemblies from Unusual α-Sheet Conformations Based on Alternation of d/l Amino Acids.

Peptide self-assembly is a hierarchical process during which secondary structures formed in the initial stages play a critical role in determining the subsequent assembling processes and final structural ordering. Unusual secondary structures hold promise as a source to develop novel supramolecular architectures with unique properties. In this work, we report the design of a new peptide self-assembly strategy based on unusual α-sheet secondary structures.