The self-assembly of low-molecular-weight building motifs into supramolecular polymers
has unlocked a new realm of materials with distinct properties and tremendous potential for …

Glycine rich polyproline II helix assemblies are an emerging class of natural domains found
in several proteins with different functions and diverse origins. The distinct properties of …

Rapid cellular uptake of synthetic molecules remains a challenge, and the motif frequently
employed to generate prodrugs, succinic ester, unfortunately lowers the efficacy of the …

The objective of this perspective on supramolecular polymers is to highlight how their
dynamic nature based on noncovalent bonding among monomers can have a profound …

Protein functions are enabled by their perfectly arranged 3D structure, which is the result of a
hierarchical intramolecular folding process. Sequence‐defined polypeptide chains form …

The most abundant natural collagens form heterotrimeric triple helices. Synthetic mimics of
collagen heterotrimers have been found to fold slowly, even compared to the already slow …

Conspectus Facilitated by the unique triple-helical protein structure, fibrous collagens, the
principal proteins in animals, demonstrate a dual function of serving as building blocks for …

The de novo design of self-assembling peptides has garnered significant attention in
scientific research. While alpha-helical assemblies have been extensively studied …

Glycine rich polyproline II helix assemblies are an emerging class of natural domains found
in several proteins with different functions and diverse origins. The distinct properties of …

Poly-L-hydroxyproline (PHyp) is a synthetic analogue of collagen, the most abundant protein
for animals, and holds immense potential for broad biomedical applications. The synthesis …