The preferred conformations of peptides heavily based on the currently extensively exploited
achiral and chiral α‐amino acids with a quaternary α‐carbon atom, as determined by …

The construction of complex protein folds relies on the precise conversion of a linear
polypeptide chain into a compact 3-dimensional structure. The interplay of forces that link …

Synthetic tripeptide based noncytotoxic hydrogelators have been discovered for releasing
an anticancer drug at physiological pH and temparature. Interestingly, gel stiffness, drug …

Here, we report two synthetic oligopeptide-based, thermoreversible, pH-sensitive hydrogels.
In gel phase, these self-assembling tetrapeptides form a long interconnected nanofibrilar …

A long-chain amino acid containing dipeptide has been found to form a hydrogel in
phosphate buffer whose pH ranges from 6.0 to 8.8. The hydrogel formed at pH 7.46 has …

Helicity is a widespread characteristic of the secondary structure of peptides: those built of L-
amino acids typically adopt right-handed helical structures, even when most of the chain is …

Two water‐soluble 310‐helical peptides are synthesized and fully characterized for the first
time. The sequence of these terminally blocked heptamers comprises two residues of the Cα …

Fibrin hydrogels made by self-assembly of fibrinogen obtained from human plasma have
shown excellent biocompatible and biodegradable properties and are widely used in …

The pH‐induced self‐assembly of three synthetic tripeptides in water medium is used to
immobilize luminescent CdS nanoparticles. These peptides form a nanofibrillar network …

Stable helical molecular structures are ubiquitous in both biological and synthetic
polymers,[1] and in general the handedness (screw-sense) of a helical polymer is dictated …