The preparation of the large molecules required for molecular recognition studies in
practical quantities is possible by assembling large building blocks with the desired …

Isolated short peptides usually are unable to maintain their original secondary structures
due to the lack of the restriction from proteins. Here we show that two complementary …

Small α/γ-peptides alternating α-aminoisobutyric acid and cyclic γ-amino acid residues are
described. NMR studies together with restrained simulated annealing revealed that an …

The α helix is an essential secondary structural motif in proteins. In particular, α helices at
the outer surface of proteins play an important role in specific biomolecular recognition …

A series of nine, frustrated, multidomain peptides is described in which forces favoring self-
assembly into a nanofiber versus those favoring disassembly could be easily modified. The …

Pepped up polymers: The synthesis and properties of novel chiral cyclic peptides designed
to complex with suitable polymers through hydrogen bonding are described. A substituted …

The de novo design of peptides and proteins has emerged as an approach for investigating
protein structure and function. The success relies heavily on the ability to design relatively …

A new capsule based on a β-sheet self-assembling cyclic peptide with the ability to
recognize and release several guests is described. The host structure is composed of two …

Natural biopolymers fold with fidelity, burying diverse side chains into well-packed cores and
protecting their backbones from solvent. Certain β-peptide oligomers assemble into bundles …

Peptide self-assembled nanostructures have attracted attention recently owing to their
promising applications in diversified avenues. To validate the importance of sidechains in …